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Conserved domains on  [gi|299473802|ref|NP_081144|]
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protein ABHD13 [Mus musculus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11437497)

alpha/beta 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
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
76-317 1.92e-56

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 183.96  E-value: 1.92e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  76 LYVPMPtGIPHENIFIRTKDGVRLNLILVRYTGDNSPYcPTIIYFHGNAGNIGHRLPNALlMLVNLRVNLVLVDYRGYGK 155
Cdd:COG1073    1 IFPPSD-KVNKEDVTFKSRDGIKLAGDLYLPAGASKKY-PAVVVAHGNGGVKEQRALYAQ-RLAELGFNVLAFDYRGYGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 156 SEGEASEEGLY--LDSEAVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENsHRISAIMVENTFLSIPHMASTLFSFF 233
Cdd:COG1073   78 SEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLEDLAAQRAKEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 234 PMRYLPLWCYK----------NKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIFPDGTHNDT-W 302
Cdd:COG1073  157 RGAYLPGVPYLpnvrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP-KELLIVPGAGHVDLyD 235
                        250
                 ....*....|....*.
gi 299473802 303 QCQG-YFTALEQFIKE 317
Cdd:COG1073  236 RPEEeYFDKLAEFFKK 251
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
76-317 1.92e-56

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 183.96  E-value: 1.92e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  76 LYVPMPtGIPHENIFIRTKDGVRLNLILVRYTGDNSPYcPTIIYFHGNAGNIGHRLPNALlMLVNLRVNLVLVDYRGYGK 155
Cdd:COG1073    1 IFPPSD-KVNKEDVTFKSRDGIKLAGDLYLPAGASKKY-PAVVVAHGNGGVKEQRALYAQ-RLAELGFNVLAFDYRGYGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 156 SEGEASEEGLY--LDSEAVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENsHRISAIMVENTFLSIPHMASTLFSFF 233
Cdd:COG1073   78 SEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLEDLAAQRAKEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 234 PMRYLPLWCYK----------NKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIFPDGTHNDT-W 302
Cdd:COG1073  157 RGAYLPGVPYLpnvrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP-KELLIVPGAGHVDLyD 235
                        250
                 ....*....|....*.
gi 299473802 303 QCQG-YFTALEQFIKE 317
Cdd:COG1073  236 RPEEeYFDKLAEFFKK 251
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
149-298 3.48e-13

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: 68.01  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTR-PDLdktKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIP 223
Cdd:pfam12146  38 DHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  224 H---------MASTLFSFFPMRYLPlWCYKNKFLS---------------------------YRKISQC-------RMPS 260
Cdd:pfam12146 115 PylappilklLAKLLGKLFPRLRVP-NNLLPDSLSrdpevvaayaadplvhggisartlyelLDAGERLlrraaaiTVPL 193
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 299473802  261 LFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:pfam12146 194 LLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
148-298 6.52e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 41.28  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 148 VDYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTRPDLDKTKVFLFGRSLGGAVA--IHLASENSH----------RIS 211
Cdd:PLN02385 121 MDYPGFGLSEGLhgyiPSFDDLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVAlkVHLKQPNAWdgailvapmcKIA 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 212 AIMVEN-TFLSIPHMASTLF---SFFPMRYLPLWCY----KNKFLSYRKIS---QCRM---------------------- 258
Cdd:PLN02385 201 DDVVPPpLVLQILILLANLLpkaKLVPQKDLAELAFrdlkKRKMAEYNVIAykdKPRLrtavellrttqeiemqleevsl 280
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 299473802 259 PSLFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:PLN02385 281 PLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYH 320
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
76-317 1.92e-56

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 183.96  E-value: 1.92e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  76 LYVPMPtGIPHENIFIRTKDGVRLNLILVRYTGDNSPYcPTIIYFHGNAGNIGHRLPNALlMLVNLRVNLVLVDYRGYGK 155
Cdd:COG1073    1 IFPPSD-KVNKEDVTFKSRDGIKLAGDLYLPAGASKKY-PAVVVAHGNGGVKEQRALYAQ-RLAELGFNVLAFDYRGYGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 156 SEGEASEEGLY--LDSEAVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENsHRISAIMVENTFLSIPHMASTLFSFF 233
Cdd:COG1073   78 SEGEPREEGSPerRDARAAVDYLRTLPGVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLEDLAAQRAKEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 234 PMRYLPLWCYK----------NKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIFPDGTHNDT-W 302
Cdd:COG1073  157 RGAYLPGVPYLpnvrlasllnDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP-KELLIVPGAGHVDLyD 235
                        250
                 ....*....|....*.
gi 299473802 303 QCQG-YFTALEQFIKE 317
Cdd:COG1073  236 RPEEeYFDKLAEFFKK 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
91-320 4.11e-33

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 122.43  E-value: 4.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  91 IRTKDGVRLNLILVRYTgDNSPYcPTIIYFHGNAGNIGHRLPNALLMLVNLRVNLVLVDYRGYGKSEGEASEEGLYlDSE 170
Cdd:COG1506    2 FKSADGTTLPGWLYLPA-DGKKY-PVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVD-DVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 171 AVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIPHMASTLFSFFPMRYLPLWcykNKFLSY 250
Cdd:COG1506   79 AAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPW---EDPEAY 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 299473802 251 RKIS------QCRMPSLFISGLSDQLIPPVMMKQLYE--LSPSRTKRLAIFPDGTHNDTWQCQ-GYFTALEQFIKEVIK 320
Cdd:COG1506  156 AARSplayadKLKTPLLLIHGEADDRVPPEQAERLYEalKKAGKPVELLVYPGEGHGFSGAGApDYLERILDFLDRHLK 234
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
85-317 4.39e-24

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 98.15  E-value: 4.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  85 PHENIFIRTKDGVRLNLilVRYTGDNSPyCPTIIYFHGNAGNIG--HRLPNALlmlVNLRVNLVLVDYRGYGKSEGE--- 159
Cdd:COG2267    2 TRRLVTLPTRDGLRLRG--RRWRPAGSP-RGTVVLVHGLGEHSGryAELAEAL---AAAGYAVLAFDLRGHGRSDGPrgh 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 160 -ASEEGLYLDSEAVLDYVMTRPDLdktKVFLFGRSLGGAVAIHLASENSHRISAIMventfLSIPHMASTLFSFFPMRYL 238
Cdd:COG2267   76 vDSFDDYVDDLRAALDALRARPGL---PVVLLGHSMGGLIALLYAARYPDRVAGLV-----LLAPAYRADPLLGPSARWL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 239 plwcykNKFLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRtKRLAIFPDGTH---NDTWQCQgYFTALEQFI 315
Cdd:COG2267  148 ------RALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPD-VELVLLPGARHellNEPAREE-VLAAILAWL 219

                 ..
gi 299473802 316 KE 317
Cdd:COG2267  220 ER 221
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
95-318 1.55e-18

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: 82.74  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  95 DGVRLNlilVRYTGDNSPycpTIIYFHGNAGNIGHRLPNALLMLVNLRVnlVLVDYRGYGKSEGEASEEGLYLDSEAVLD 174
Cdd:COG0596   10 DGVRLH---YREAGPDGP---PVVLLHGLPGSSYEWRPLIPALAAGYRV--IAPDLRGHGRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 175 yVMTRpdLDKTKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIPHMASTLFSFFPMRYLPLWCYKNKFLSYRKIS 254
Cdd:COG0596   82 -LLDA--LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALAALLRALARTDLRERLA 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 299473802 255 QCRMPSLFISGLSDQLIPPVMMKQLYELSPsrTKRLAIFPDGTHNDTWQCQGYFT-ALEQFIKEV 318
Cdd:COG0596  159 RITVPTLVIWGEKDPIVPPALARRLAELLP--NAELVVLPGAGHFPPLEQPEAFAaALRDFLARL 221
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
149-298 3.48e-13

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: 68.01  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  149 DYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTR-PDLdktKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFLSIP 223
Cdd:pfam12146  38 DHRGHGRSDGKrghvPSFDDYVDDLDTFVDKIREEhPGL---PLFLLGHSMGGLIAALYALRYPDKVDGLILSAPALKIK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  224 H---------MASTLFSFFPMRYLPlWCYKNKFLS---------------------------YRKISQC-------RMPS 260
Cdd:pfam12146 115 PylappilklLAKLLGKLFPRLRVP-NNLLPDSLSrdpevvaayaadplvhggisartlyelLDAGERLlrraaaiTVPL 193
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 299473802  261 LFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:pfam12146 194 LLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYH 231
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
115-238 2.25e-09

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: 57.13  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  115 PTIIYFHGNAGNIG--HRLPNALLmlvNLRVNLVLVDYRGYGKSEGEASEEGLYLDS-EAVLDYVMTRpdLDKTKVFLFG 191
Cdd:pfam00561   1 PPVLLLHGLPGSSDlwRKLAPALA---RDGFRVIALDLRGFGKSSRPKAQDDYRTDDlAEDLEYILEA--LGLEKVNLVG 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 299473802  192 RSLGGAVAIHLASENSHRISAIMVENTFLSiPHMASTLFSFFPMRYL 238
Cdd:pfam00561  76 HSMGGLIALAYAAKYPDRVKALVLLGALDP-PHELDEADRFILALFP 121
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
117-320 5.51e-09

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 56.10  E-value: 5.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 117 IIYFHGNAGN------IGHRLpnallmlVNLRVNLVLVDYRGYGKSEGEASE---EGLYLDSEAVLDYVMTRPDldktKV 187
Cdd:COG1647   18 VLLLHGFTGSpaemrpLAEAL-------AKAGYTVYAPRLPGHGTSPEDLLKttwEDWLEDVEEAYEILKAGYD----KV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 188 FLFGRSLGGAVAIHLASENSHrISAIMVENTFLSIPHMASTLFSFFPM----------------------RYLPLWCYKN 245
Cdd:COG1647   87 IVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSAPLLPLLKYlarslrgigsdiedpevaeyayDRTPLRALAE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 246 --KFLSY--RKISQCRMPSLFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTHNDT--WQCQGYFTALEQFIKEVI 319
Cdd:COG1647  166 lqRLIREvrRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVITldKDREEVAEEILDFLERLA 245

                 .
gi 299473802 320 K 320
Cdd:COG1647  246 A 246
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
84-298 1.20e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 54.59  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  84 IPHENIFIRTKDGVRLNLILVRYTGDnSPYcPTIIYFHGNAGnIGHRLPNALLMLVNLRVNLVLVDY---RGYGKSEGEA 160
Cdd:COG0412    1 MTTETVTIPTPDGVTLPGYLARPAGG-GPR-PGVVVLHEIFG-LNPHIRDVARRLAAAGYVVLAPDLygrGGPGDDPDEA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 161 SEEGLYLDSE-------AVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENsHRISAImventflsiphmastlFSFF 233
Cdd:COG0412   78 RALMGALDPEllaadlrAALDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARG-PDLAAA----------------VSFY 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 299473802 234 PMRYLPlwcyknkfLSYRKISQCRMPSLFISGLSDQLIPPVMMKQLYEL--SPSRTKRLAIFPDGTH 298
Cdd:COG0412  141 GGLPAD--------DLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAAlaAAGVDVELHVYPGAGH 199
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
141-298 8.69e-08

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 51.70  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 141 LRVNlvlvdYRGYGKSEGEASE-EGLYLDSEAVLDYVMTRPDLdktKVFLFGRSLGGAVAIHLASEnSHRISAimventF 219
Cdd:COG2945   59 LRFN-----FRGVGRSEGEFDEgRGELDDAAAALDWLRAQNPL---PLWLAGFSFGAYVALQLAMR-LPEVEG------L 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 220 LSIphmaSTLFSFFPMRYLPLwcyknkflsyrkisqCRMPSLFISGLSDQLIPPVMMKQLYE-LSPsrTKRLAIFPDGTH 298
Cdd:COG2945  124 ILV----APPVNRYDFSFLAP---------------CPAPTLVIHGEQDEVVPPAEVLDWARpLSP--PLPVVVVPGADH 182
Axe1 COG3458
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, ...
78-298 1.50e-06

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


Pssm-ID: 442681 [Multi-domain]  Cd Length: 318  Bit Score: 49.03  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  78 VPMPTGIPHENIF---IRTKDGVRLNLILVRYTGDNsPYcPTIIYFHGNAGNIGhrLPNALLMLVNLRVNLVLVDYRGYG 154
Cdd:COG3458   45 TPVETGLPGVEVYdvtFTGFGGARIYGWLLRPKGEG-PL-PAVVEFHGYGGGRG--LPHEDLDWAAAGYAVLVMDTRGQG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 155 KSEGEASEE-------------------------GLYLDseAV--LDYVMTRPDLDKTKVFLFGRSLGGAVAIhLASENS 207
Cdd:COG3458  121 SSWGDTPDPggysggalpgymtrgiddpdtyyyrRVYLD--AVraVDALRSLPEVDGKRIGVTGGSQGGGLAL-AAAALD 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 208 HRISAIMVENTFLS-IP---HMAST-----LFSFFPMRYLPlwcYKNKF--LSY-------RKIsqcRMPSLFISGLSDQ 269
Cdd:COG3458  198 PRVKAAAADVPFLCdFRralELGRAgpypeIRRYLRRHRER---EPEVFetLSYfdavnfaRRI---KAPVLFSVGLMDP 271
                        250       260
                 ....*....|....*....|....*....
gi 299473802 270 LIPPVMMKQLYELSPSrTKRLAIFPDGTH 298
Cdd:COG3458  272 VCPPSTVFAAYNALAG-PKEILVYPFNGH 299
YpfH COG0400
Predicted esterase [General function prediction only];
115-282 2.77e-06

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 47.21  E-value: 2.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 115 PTIIYFHGNAGN------IGHRL--PNALLMLVNLRVNLVLVDYR--GYGKSEGEASEEGL-----YLDseAVLDYVMTR 179
Cdd:COG0400    6 PLVVLLHGYGGDeedllpLAPELalPGAAVLAPRAPVPEGPGGRAwfDLSFLEGREDEEGLaaaaeALA--AFIDELEAR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 180 PDLDKTKVFLFGRSLGGAVAIHLASENSHRISAIMventflsiphmastLFS-FFPMRylPLWCYKNKFLSYRKIsqcrm 258
Cdd:COG0400   84 YGIDPERIVLAGFSQGAAMALSLALRRPELLAGVV--------------ALSgYLPGE--EALPAPEAALAGTPV----- 142
                        170       180
                 ....*....|....*....|....
gi 299473802 259 psLFISGLSDQLIPPVMMKQLYEL 282
Cdd:COG0400  143 --FLAHGTQDPVIPVERAREAAEA 164
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
117-226 3.75e-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: 44.00  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  117 IIYFHGNAGNIGHrlpnaLLMLVNLRVNLVLVDYRGYGKSEGEASEEGLYLDSEAVLDYVmtrpdLDKTKVFLFGRSLGG 196
Cdd:pfam12697   1 VVLVHGAGLSAAP-----LAALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDEL-----GAARPVVLVGHSLGG 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 299473802  197 AVAIHLAseNSHRISAIMVENTFLSIPHMA 226
Cdd:pfam12697  71 AVALAAA--AAALVVGVLVAPLAAPPGLLA 98
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
148-298 6.52e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 41.28  E-value: 6.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 148 VDYRGYGKSEGE----ASEEGLYLDSEAVLDYVMTRPDLDKTKVFLFGRSLGGAVA--IHLASENSH----------RIS 211
Cdd:PLN02385 121 MDYPGFGLSEGLhgyiPSFDDLVDDVIEHYSKIKGNPEFRGLPSFLFGQSMGGAVAlkVHLKQPNAWdgailvapmcKIA 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 212 AIMVEN-TFLSIPHMASTLF---SFFPMRYLPLWCY----KNKFLSYRKIS---QCRM---------------------- 258
Cdd:PLN02385 201 DDVVPPpLVLQILILLANLLpkaKLVPQKDLAELAFrdlkKRKMAEYNVIAykdKPRLrtavellrttqeiemqleevsl 280
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 299473802 259 PSLFISGLSDQLIPPVMMKQLYELSPSRTKRLAIFPDGTH 298
Cdd:PLN02385 281 PLLILHGEADKVTDPSVSKFLYEKASSSDKKLKLYEDAYH 320
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
171-215 2.62e-03

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 38.83  E-value: 2.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 299473802 171 AVLDYVMTRPDLDKTKVFLFGRSLGGAVAIHLASENSHRISAIMV 215
Cdd:COG3509  120 ALVDDLAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAP 164
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
115-214 4.17e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 37.93  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802 115 PTIIYFHG---NAGNIGHRLPNALLMLVNLRVNLVLVDYRgygkSEGEASEEGLYLDSEAVLDYVMTRPD---LDKTKVF 188
Cdd:COG0657   14 PVVVYFHGggwVSGSKDTHDPLARRLAARAGAAVVSVDYR----LAPEHPFPAALEDAYAALRWLRANAAelgIDPDRIA 89
                         90       100       110
                 ....*....|....*....|....*....|
gi 299473802 189 LFGRSLGG----AVAIHLASENSHRISAIM 214
Cdd:COG0657   90 VAGDSAGGhlaaALALRARDRGGPRPAAQV 119
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
117-203 7.75e-03

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: 37.19  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  117 IIYFHGNAGNIGH-RLPNALLML--VNLRVNLVLVDYRgygksegEASE---EGLYLDSEAVLDYVMTRPDL---DKTKV 187
Cdd:pfam07859   1 LVYFHGGGFVLGSaDTHDRLCRRlaAEAGAVVVSVDYR-------LAPEhpfPAAYDDAYAALRWLAEQAAElgaDPSRI 73
                          90
                  ....*....|....*.
gi 299473802  188 FLFGRSLGGAVAIHLA 203
Cdd:pfam07859  74 AVAGDSAGGNLAAAVA 89
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
111-319 8.21e-03

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: 36.97  E-value: 8.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  111 SPYCPTIIYFHG---------NAGNIGHRLPNALLMLVNLRVNLVLVDYRG--------YGKSEGEASEEGLYLDS---- 169
Cdd:pfam02230  11 DPAQATVIFLHGlgdsghgwaDAAKTEAPLPNIKFIFPHGPEIPVTLNGGMrmpawfdlVGLSPNAKEDEAGIKNSaeti 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299473802  170 EAVLDYVMTRPdLDKTKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFLsIPHMAstlfsfFPmrylplwcyKNKFLS 249
Cdd:pfam02230  91 EELIDAEQKKG-IPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFL-PLPTK------FP---------SHPNLV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 299473802  250 YRKISQCRmpslfISGLSDQLIPPVMMKQLYELSPSRTKR--LAIFPDGTHNdtwQCQGYFTALEQFIKEVI 319
Cdd:pfam02230 154 TKKTPIFL-----IHGEEDPVVPLALGKLAKEYLKTSLNKveLKIYEGLAHS---ICGREMQDIKKFLSKHI 217
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
182-220 9.68e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 37.26  E-value: 9.68e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 299473802 182 LDKTKVFLFGRSLGGAVAIHLASENSHRISAIMVENTFL 220
Cdd:PRK00870 112 LDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANTGL 150
 
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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