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Conserved domains on  [gi|530360807|ref|XP_005245785|]
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acyl-protein thioesterase 2 isoform X1 [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10491393)

alpha/beta hydrolase similar to acyl-protein thioesterase that hydrolyzes fatty acids from S-acylated cysteine residues in proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
23-240 1.87e-113

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


:

Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 323.94  E-value: 1.87e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   23 LTDAATVSGAERETAAVIFLHGLGDTGHSWADALST-IRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDE 101
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKTeAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  102 AGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAIL 181
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVTKKTPIF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807  182 QCHGELDPMVPVRFGALTAEKLRSVVTpaRVQFKTYPGVMHSSCPQEMAAVKEFLEKLL 240
Cdd:pfam02230 161 LIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
23-240 1.87e-113

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 323.94  E-value: 1.87e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   23 LTDAATVSGAERETAAVIFLHGLGDTGHSWADALST-IRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDE 101
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKTeAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  102 AGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAIL 181
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVTKKTPIF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807  182 QCHGELDPMVPVRFGALTAEKLRSVVTpaRVQFKTYPGVMHSSCPQEMAAVKEFLEKLL 240
Cdd:pfam02230 161 LIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
32-241 2.03e-52

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 168.55  E-value: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  32 AERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAPRIPVtlnmkMVMPSWFDLMGLSPDapEDEAGIKKAAENI 111
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFLEGR--EDEEGLAAAAEAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 112 KALIEHEMKN-GIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLhRAFPQAANGSAKDLAILQCHGELDPM 190
Cdd:COG0400   74 AAFIDELEARyGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPG-EEALPAPEAALAGTPVFLAHGTQDPV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530360807 191 VPVRFGALTAEKLRSvvTPARVQFKTYPGvMHSSCPQEMAAVKEFLEKLLP 241
Cdd:COG0400  153 IPVERAREAAEALEA--AGADVTYREYPG-GHEISPEELADARAWLAERLA 200
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
31-158 1.61e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 39.45  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   31 GAERETAAVIFLHGLGDTGHSWadalstirLPHVKYICPHAPRIPVtlnmkmvmpswfDLMG---------LSPDAPEDE 101
Cdd:PLN02980 1366 GQNAEGSVVLFLHGFLGTGEDW--------IPIMKAISGSARCISI------------DLPGhggskiqnhAKETQTEPT 1425
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530360807  102 AGIKKAAENIKALIEHemkngIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALS 158
Cdd:PLN02980 1426 LSVELVADLLYKLIEH-----ITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIIS 1477
 
Name Accession Description Interval E-value
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
23-240 1.87e-113

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 323.94  E-value: 1.87e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   23 LTDAATVSGAERETAAVIFLHGLGDTGHSWADALST-IRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDE 101
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKTeAPLPNIKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  102 AGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAIL 181
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVTKKTPIF 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807  182 QCHGELDPMVPVRFGALTAEKLRSVVTpaRVQFKTYPGVMHSSCPQEMAAVKEFLEKLL 240
Cdd:pfam02230 161 LIHGEEDPVVPLALGKLAKEYLKTSLN--KVELKIYEGLAHSICGREMQDIKKFLSKHI 217
YpfH COG0400
Predicted esterase [General function prediction only];
32-241 2.03e-52

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 168.55  E-value: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  32 AERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAPRIPVtlnmkMVMPSWFDLMGLSPDapEDEAGIKKAAENI 111
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAAVLAPRAPVPEG-----PGGRAWFDLSFLEGR--EDEEGLAAAAEAL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 112 KALIEHEMKN-GIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLhRAFPQAANGSAKDLAILQCHGELDPM 190
Cdd:COG0400   74 AAFIDELEARyGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPG-EEALPAPEAALAGTPVFLAHGTQDPV 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530360807 191 VPVRFGALTAEKLRSvvTPARVQFKTYPGvMHSSCPQEMAAVKEFLEKLLP 241
Cdd:COG0400  153 IPVERAREAAEALEA--AGADVTYREYPG-GHEISPEELADARAWLAERLA 200
COG4099 COG4099
Predicted peptidase [General function prediction only];
39-224 1.90e-15

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 73.08  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  39 VIFLHGLGDTGHswaDALSTIRLPHVKYICP-HAPRIPVtlnmkMVmpswfdlmgLSPDAPEDEA-GIKKAAENIKALIE 116
Cdd:COG4099   52 VLFLHGAGERGT---DNEKQLTHGAPKFINPeNQAKFPA-----IV---------LAPQCPEDDYwSDTKALDAVLALLD 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 117 HEMKN-GIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWlplhrAFPQAANgSAKDLAILQCHGELDPMVPVRF 195
Cdd:COG4099  115 DLIAEyRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICGG-----GDPANAA-NLKKVPVWIFHGAKDDVVPVEE 188
                        170       180
                 ....*....|....*....|....*....
gi 530360807 196 GALTAEKLRSVvtPARVQFKTYPGVMHSS 224
Cdd:COG4099  189 SRAMVEALKAA--GADVKYTEYPGVGHNS 215
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
32-238 1.22e-12

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 65.02  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  32 AERETAAVIFLHGLGDTGHSW---ADALstirlphvkyicpHAPRIPVTLnmkmvmpswFDL--MGLSPDAPEDEAGIKK 106
Cdd:COG2267   24 AGSPRGTVVLVHGLGEHSGRYaelAEAL-------------AAAGYAVLA---------FDLrgHGRSDGPRGHVDSFDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 107 AAENIKALIEHEMKNgiPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALS---CWLPLH-------RAFPQAANGSAK 176
Cdd:COG2267   82 YVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLApayRADPLLgpsarwlRALRLAEALARI 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360807 177 DLAILQCHGELDPMVPVRFGALTAEKLrsvvtPARVQFKTYPG----VMHSSCPQE-MAAVKEFLEK 238
Cdd:COG2267  160 DVPVLVLHGGADRVVPPEAARRLAARL-----SPDVELVLLPGarheLLNEPAREEvLAAILAWLER 221
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
38-239 4.25e-11

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: 60.79  E-value: 4.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  38 AVIFLHGLGDTGHSW---ADALStirlPHVKYICPhapripvtlnmkmvmpswfDL--MGLSpDAPEDEAGIKKAAENIK 112
Cdd:COG0596   25 PVVLLHGLPGSSYEWrplIPALA----AGYRVIAP-------------------DLrgHGRS-DKPAGGYTLDDLADDLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 113 ALIEHEmknGIPanRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWL---------------PLHRAFPQAANGSAKD 177
Cdd:COG0596   81 ALLDAL---GLE--RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLaalaeplrrpglapeALAALLRALARTDLRE 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530360807 178 LA------ILQCHGELDPMVPVRFGALTAEKLRsvvtpaRVQFKTYPGV---MHSSCPQEMA-AVKEFLEKL 239
Cdd:COG0596  156 RLaritvpTLVIWGEKDPIVPPALARRLAELLP------NAELVVLPGAghfPPLEQPEAFAaALRDFLARL 221
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
95-240 9.34e-09

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 53.72  E-value: 9.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  95 PDAPED-EAGIKKAAENIKALiehemknGIPANRIVLGGFSQGGALSLYTALTCPHP----LAGIVALSCWLPLhRAFPq 169
Cdd:COG0657   61 PAALEDaYAALRWLRANAAEL-------GIDPDRIAVAGDSAGGHLAAALALRARDRggprPAAQVLIYPVLDL-TASP- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 170 aANGSAKDLA-ILQCHGELDPMvpVRFGALTAEKLRSVVTParVQFKTYPGVMHSSC--------PQEMAAVKEFLEKLL 240
Cdd:COG0657  132 -LRADLAGLPpTLIVTGEADPL--VDESEALAAALRAAGVP--VELHVYPGGGHGFGllaglpeaRAALAEIAAFLRRAL 206
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
83-223 2.35e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 53.05  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  83 VMPSWFDlmGLSPDAPEDEAG-------IKKAAENIKALIEHEMKN-GIPANRIVLGGFSQGGALSLYTALTCPhPLAGI 154
Cdd:COG0412   60 LAPDLYG--RGGPGDDPDEARalmgaldPELLAADLRAALDWLKAQpEVDAGRVGVVGFCFGGGLALLAAARGP-DLAAA 136
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807 155 VALSCWLPLHRAFPQAANGSAKdlaILQCHGELDPMVPVRFGALTAEKLRSvvTPARVQFKTYPGVMHS 223
Cdd:COG0412  137 VSFYGGLPADDLLDLAARIKAP---VLLLYGEKDPLVPPEQVAALEAALAA--AGVDVELHVYPGAGHG 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
111-241 2.63e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 50.02  E-value: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 111 IKALIEHemkNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSC------WLPLHRAFPQAANGSAKDLAI---- 180
Cdd:COG1506   81 IDYLAAR---PYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGvsdlrsYYGTTREYTERLMGGPWEDPEayaa 157
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807 181 ---------LQC-----HGELDPMVPVRFGALTAEKLRSvvTPARVQFKTYPGVMH----SSCPQEMAAVKEFLEKLLP 241
Cdd:COG1506  158 rsplayadkLKTpllliHGEADDRVPPEQAERLYEALKK--AGKPVELLVYPGEGHgfsgAGAPDYLERILDFLDRHLK 234
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
39-219 1.47e-06

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 48.31  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  39 VIFLHGLGDTGHSWADALstiRLPHV--KYIcpHAPRIPVTLnmkMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIE 116
Cdd:COG2382  115 LYLLDGGGGDEQDWFDQG---RLPTIldNLI--AAGKIPPMI---VVMPDGGDGGDRGTEGPGNDAFERFLAEELIPFVE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 117 HEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALS---CWLPLHRAFPQ-----AANGSAKDLAILQCHGELD 188
Cdd:COG2382  187 KNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSgsfWWPPGDADRGGwaellAAGAPKKPLRFYLDVGTED 266
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530360807 189 PMVPvrfgalTAEKLRSVVTPA--RVQFKTYPG 219
Cdd:COG2382  267 DLLE------ANRALAAALKAKgyDVEYREFPG 293
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
38-158 2.41e-06

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: 47.11  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   38 AVIFLHGLGDTGHSWADALSTIRLPHVKYICphapripvtlnmkmvmpswFDLMGL--SPDAPEDEAGIKKA-AENIKAL 114
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIA-------------------LDLRGFgkSSRPKAQDDYRTDDlAEDLEYI 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530360807  115 IEHemkNGIPanRIVLGGFSQGGALSLYTALTCPHPLAGIVALS 158
Cdd:pfam00561  63 LEA---LGLE--KVNLVGHSMGGLIALAYAAKYPDRVKALVLLG 101
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
37-206 3.40e-06

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 46.92  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  37 AAVIFLHGLGDTG---------HSWADALSTIrlphVKYicPHAPRipvtlnmKMVMPSWFDLMGLSPDAPEDEAGIkka 107
Cdd:COG3509   54 PLVVALHGCGGSAadfaagtglNALADREGFI----VVY--PEGTG-------RAPGRCWNWFDGRDQRRGRDDVAF--- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 108 aenIKALIEHEMKN-GIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCwLPLHRAFPQAANgSAKDLAILQCHGE 186
Cdd:COG3509  118 ---IAALVDDLAARyGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAG-LPYGAASDAACA-PGRPVPVLVIHGT 192
                        170       180
                 ....*....|....*....|
gi 530360807 187 LDPMVPVRFGALTAEKLRSV 206
Cdd:COG3509  193 ADPTVPYAGAEETLAQWAAL 212
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
39-192 3.66e-04

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 40.34  E-value: 3.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   39 VIFLHGLGDTGHSWADALSTIRlPHVK------------YICPHAPRIPVTLNMKMVMP------SWFdlmgLSPDAPED 100
Cdd:pfam03959   6 VLCLHGFGQSGEIFRAKTGALR-KLLKklgvefvyldapFELAEPADLPGSESEKDEGEddepyrAWF----FGDDDTNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  101 EAGIKKAaenIKALIEHEMKNGiPANRIVlgGFSQGGALSLYTA------LTCPHP-LAGIVALSCWLPLHRAFPQAANG 173
Cdd:pfam03959  81 YLGLDES---LDYVRDYIKENG-PFDGIL--GFSQGAALAAILAslleegLPLSHPpLKFAILFSGFRPRPPIYQEYYSE 154
                         170
                  ....*....|....*....
gi 530360807  174 SAKDLAILQCHGELDPMVP 192
Cdd:pfam03959 155 DPIQTPSLHVIGELDTVVP 173
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
38-239 5.88e-04

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 39.92  E-value: 5.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807  38 AVIFLHGLGDTGHS---WADAL-------STIRLP-HvkyicphapripvtlnmkmvmpswfdlmGLSPDAPEdEAGIKK 106
Cdd:COG1647   17 GVLLLHGFTGSPAEmrpLAEALakagytvYAPRLPgH----------------------------GTSPEDLL-KTTWED 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 107 AAENIKALIEhEMKNGipANRIVLGGFSQGGALSLYTALTCPHpLAGIVALS-------------CWLPLHRAFPQAANG 173
Cdd:COG1647   68 WLEDVEEAYE-ILKAG--YDKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSpalkiddpsapllPLLKYLARSLRGIGS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807 174 SAKD------------------LAILQC----------------HGELDPMVPVRFGALTAEKLRSvvtpARVQFKTYPG 219
Cdd:COG1647  144 DIEDpevaeyaydrtplralaeLQRLIRevrrdlpkitaptliiQSRKDEVVPPESARYIYERLGS----PDKELVWLED 219
                        250       260
                 ....*....|....*....|....*
gi 530360807 220 ---VMHSSCPQE--MAAVKEFLEKL 239
Cdd:COG1647  220 sghVITLDKDREevAEEILDFLERL 244
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
31-158 1.61e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 39.45  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360807   31 GAERETAAVIFLHGLGDTGHSWadalstirLPHVKYICPHAPRIPVtlnmkmvmpswfDLMG---------LSPDAPEDE 101
Cdd:PLN02980 1366 GQNAEGSVVLFLHGFLGTGEDW--------IPIMKAISGSARCISI------------DLPGhggskiqnhAKETQTEPT 1425
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530360807  102 AGIKKAAENIKALIEHemkngIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALS 158
Cdd:PLN02980 1426 LSVELVADLLYKLIEH-----ITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIIS 1477
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
93-146 7.86e-03

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 36.39  E-value: 7.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530360807   93 LSPDAP-----EDeagIKKAaenIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALT 146
Cdd:pfam20434  57 LSTDAKfpaqiQD---VKAA---IRFLRANAAKYGIDTNKIALMGFSAGGHLALLAGLS 109
 
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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