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Conserved domains on  [gi|1755817234|gb|QEW17907|]
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L-amino acid amidase [Marinibacterium anthonyi]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 10-298 1.65e-90

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


The actual alignment was detected with superfamily member TIGR01250:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 289  Bit Score: 270.79  E-value: 1.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  10 TEGVSPYRGYETWYRITGDLGaDKLPLVIAHGGPGCTHDYVDSFKDIAA-TGRPVIHYDQIGNGNSTRLPEKGAEFWTVD 88
Cdd:TIGR01250   3 IEGIITVDGGYHLFTKTGGEG-EKIKLLLLHGGPGMSHEYLENLRELLKeEGREVIMYDQLGCGYSDQPDDSDEELWTID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  89 FFLGELDALLDHLGIrDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRADLPEDVQEALNRHE 168
Cdd:TIGR01250  82 YFVDELEEVREKLGL-DKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKRCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 169 AAGTTSDPEYIKAQDVFYARHVCRIVPNPPEVQRTFDIMAkdSTVYNAMNGPNEFHVVGTMKTWTVIDRLDRIKVPVLAY 248
Cdd:TIGR01250 161 ASGDYDNPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGGN--TNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLT 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755817234 249 RGHYDEATEACVQPFLDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFL 298
Cdd:TIGR01250 239 VGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 10-298 1.65e-90

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 270.79  E-value: 1.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  10 TEGVSPYRGYETWYRITGDLGaDKLPLVIAHGGPGCTHDYVDSFKDIAA-TGRPVIHYDQIGNGNSTRLPEKGAEFWTVD 88
Cdd:TIGR01250   3 IEGIITVDGGYHLFTKTGGEG-EKIKLLLLHGGPGMSHEYLENLRELLKeEGREVIMYDQLGCGYSDQPDDSDEELWTID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  89 FFLGELDALLDHLGIrDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRADLPEDVQEALNRHE 168
Cdd:TIGR01250  82 YFVDELEEVREKLGL-DKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKRCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 169 AAGTTSDPEYIKAQDVFYARHVCRIVPNPPEVQRTFDIMAkdSTVYNAMNGPNEFHVVGTMKTWTVIDRLDRIKVPVLAY 248
Cdd:TIGR01250 161 ASGDYDNPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGGN--TNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLT 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755817234 249 RGHYDEATEACVQPFLDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFL 298
Cdd:TIGR01250 239 VGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-300 6.13e-29

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: 110.09  E-value: 6.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234   1 MTTDTTIPVtegvspyRGYETWYRITGDlgaDKLPLVIAHGGPGCTHDYVDSFKDIAAtGRPVIHYDQIGNGNSTRLPEK 80
Cdd:COG0596     1 MSTPRFVTV-------DGVRLHYREAGP---DGPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  81 gaefWTVDFFLGELDALLDHLGIrDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANspasmklwgegaarlradlpEDV 160
Cdd:COG0596    70 ----YTLDDLADDLAALLDALGL-ERVVLVGHSMGGMVALELAARHPERVAGLVLVD--------------------EVL 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 161 QEalnrheaagttsdpeyikaqdvfYARHVCRIVPNPPEVQRTFDIMAKdstvynamngpnefhvvgtmktWTVIDRLDR 240
Cdd:COG0596   125 AA-----------------------LAEPLRRPGLAPEALAALLRALAR----------------------TDLRERLAR 159

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755817234 241 IKVPVLAYRGHYDEAT-EACVQPFLDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFLAQ 300
Cdd:COG0596   160 ITVPTLVIWGEKDPIVpPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 35-286 7.01e-22

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: 91.80  E-value: 7.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  35 PLVIAHGGPGCTHDYVDSFKDIAATGRPVIHYDQIGNGNSTRLPEKGAefWTVDFFLGELDALLDHLGIrDRYALLGQSW 114
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGL-EKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 115 GGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRADLPEDVQEALNRHEAAGTTSDPEYIKAQDVFYARHVCRIv 194
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 195 pnpPEVQRTFDIMAKDSTVYNAMNGPNEFhvvgtmKTWTVIDR---LDRIKVPVLAYRGHYDEATEACVQPFLD-LIPDV 270
Cdd:pfam00561 158 ---PLLNKRFPSGDYALAKSLVTGALLFI------ETWSTELRakfLGRLDEPTLIIWGDQDPLVPPQALEKLAqLFPNA 228

                         250
                  ....*....|....*.
gi 1755817234 271 RGHVFPNSAHMPHVEE 286
Cdd:pfam00561 229 RLVVIPDAGHFAFLEG 244
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 31-300 4.49e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 50.71  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  31 ADKLPLVIAHGGPGCTHDYVDSFKDIAAtGRPVIHYDQIGNGNSTRLPEKGaefwTVDFFLGELDALLDHLGIrDRYALL 110
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALAA-GRPVIALDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGI-ERAHLV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 111 GQSWGGMLGAEHAVLQPRGLKALVIAnSPASMklwGEgaaRLRADLPEDVQEALNRHEaagttsdpeyIKAqdvfyarHV 190
Cdd:PRK14875  203 GHSMGGAVALRLAARAPQRVASLTLI-APAGL---GP---EINGDYIDGFVAAESRRE----------LKP-------VL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 191 CRIVPNPPEVQRTfdiMAKDSTVYNAMNGPNE---------FHvvGTMKTWTVIDRLDRIKVPVLAYRGHYDEateacVQ 261
Cdd:PRK14875  259 ELLFADPALVTRQ---MVEDLLKYKRLDGVDDalraladalFA--GGRQRVDLRDRLASLAIPVLVIWGEQDR-----II 328

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1755817234 262 PF---LDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFLAQ 300
Cdd:PRK14875  329 PAahaQGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
 
Name Accession Description Interval E-value
pro_imino_pep_2 TIGR01250
proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a ...
 10-298 1.65e-90

proline-specific peptidase, Bacillus coagulans-type subfamily; This model describes a subfamily of the alpha/beta fold family of hydrolases. Characterized members include prolinases (Pro-Xaa dipeptidase, EC 3.4.13.8), prolyl aminopeptidases (EC 3.4.11.5), and a leucyl aminopeptidase


Pssm-ID: 188121 [Multi-domain]  Cd Length: 289  Bit Score: 270.79  E-value: 1.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  10 TEGVSPYRGYETWYRITGDLGaDKLPLVIAHGGPGCTHDYVDSFKDIAA-TGRPVIHYDQIGNGNSTRLPEKGAEFWTVD 88
Cdd:TIGR01250   3 IEGIITVDGGYHLFTKTGGEG-EKIKLLLLHGGPGMSHEYLENLRELLKeEGREVIMYDQLGCGYSDQPDDSDEELWTID 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  89 FFLGELDALLDHLGIrDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRADLPEDVQEALNRHE 168
Cdd:TIGR01250  82 YFVDELEEVREKLGL-DKFYLLGHSWGGMLAQEYALKYGQHLKGLIISSMLDSAPEYVKELNRLRKELPPEVRAAIKRCE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 169 AAGTTSDPEYIKAQDVFYARHVCRIVPNPPEVQRTFDIMAkdSTVYNAMNGPNEFHVVGTMKTWTVIDRLDRIKVPVLAY 248
Cdd:TIGR01250 161 ASGDYDNPEYQEAVEVFYHHLLCRLRKWPEALKHLKSGGN--TNVYNIMQGPNEFTITGNLKDWDITDKLSEIKVPTLLT 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1755817234 249 RGHYDEATEACVQPFLDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFL 298
Cdd:TIGR01250 239 VGEFDTMTPEAAREMQELIAGSRLVVFPDGSHMTMIEDPEVYFKLLSDFI 288
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1-300 6.13e-29

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: 110.09  E-value: 6.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234   1 MTTDTTIPVtegvspyRGYETWYRITGDlgaDKLPLVIAHGGPGCTHDYVDSFKDIAAtGRPVIHYDQIGNGNSTRLPEK 80
Cdd:COG0596     1 MSTPRFVTV-------DGVRLHYREAGP---DGPPVVLLHGLPGSSYEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  81 gaefWTVDFFLGELDALLDHLGIrDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANspasmklwgegaarlradlpEDV 160
Cdd:COG0596    70 ----YTLDDLADDLAALLDALGL-ERVVLVGHSMGGMVALELAARHPERVAGLVLVD--------------------EVL 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 161 QEalnrheaagttsdpeyikaqdvfYARHVCRIVPNPPEVQRTFDIMAKdstvynamngpnefhvvgtmktWTVIDRLDR 240
Cdd:COG0596   125 AA-----------------------LAEPLRRPGLAPEALAALLRALAR----------------------TDLRERLAR 159

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1755817234 241 IKVPVLAYRGHYDEAT-EACVQPFLDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFLAQ 300
Cdd:COG0596   160 ITVPTLVIWGEKDPIVpPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 35-286 7.01e-22

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: 91.80  E-value: 7.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  35 PLVIAHGGPGCTHDYVDSFKDIAATGRPVIHYDQIGNGNSTRLPEKGAefWTVDFFLGELDALLDHLGIrDRYALLGQSW 114
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDD--YRTDDLAEDLEYILEALGL-EKVNLVGHSM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 115 GGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRADLPEDVQEALNRHEAAGTTSDPEYIKAQDVFYARHVCRIv 194
Cdd:pfam00561  79 GGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLALLLLRLRLLKAL- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 195 pnpPEVQRTFDIMAKDSTVYNAMNGPNEFhvvgtmKTWTVIDR---LDRIKVPVLAYRGHYDEATEACVQPFLD-LIPDV 270
Cdd:pfam00561 158 ---PLLNKRFPSGDYALAKSLVTGALLFI------ETWSTELRakfLGRLDEPTLIIWGDQDPLVPPQALEKLAqLFPNA 228

                         250
                  ....*....|....*.
gi 1755817234 271 RGHVFPNSAHMPHVEE 286
Cdd:pfam00561 229 RLVVIPDAGHFAFLEG 244
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
23-140 9.29e-08

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 51.54  E-value: 9.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  23 YRITGDLGADKLPLVIAHGGPGCTHDYVDSFKDIAATGRPVIHYDQIGNGNSTRLPekgAEFWTVDFFLGELDALLDHLG 102
Cdd:COG2267    18 GRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPR---GHVDSFDDYVDDLRAALDALR 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1755817234 103 IR--DRYALLGQSWGGMLGAEHAVLQPRGLKALViANSPA 140
Cdd:COG2267    95 ARpgLPVVLLGHSMGGLIALLYAARYPDRVAGLV-LLAPA 133
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 36-285 9.61e-08

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: 51.83  E-value: 9.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  36 LVIAHGGPGCTHDYVDSFKDIAATGRPVIHYDQIGNGNSTrlPEKG--AEFwtvDFFLGELDALLDHlgIRDRY-----A 108
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSD--GKRGhvPSF---DDYVDDLDTFVDK--IREEHpglplF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 109 LLGQSWGGMLGAEHAVLQPRGLKALVIAnSPA------SMKLWGEGAARLRADLPEDVQeALNRHEAAGTTSDPEYIKAq 182
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILS-APAlkikpyLAPPILKLLAKLLGKLFPRLR-VPNNLLPDSLSRDPEVVAA- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 183 dvfYARHvcrivpnpPEVQRTFDImakdSTVYNAMNGpnefhvvgtMKtwTVIDRLDRIKVPVLAYRGHYD-----EATE 257
Cdd:pfam12146 157 ---YAAD--------PLVHGGISA----RTLYELLDA---------GE--RLLRRAAAITVPLLLLHGGADrvvdpAGSR 210

                         250       260       270
                  ....*....|....*....|....*....|
gi 1755817234 258 AcvqpFLDLIP--DVRGHVFPNSAHMPHVE 285
Cdd:pfam12146 211 E----FYERAGstDKTLKLYPGLYHELLNE 236
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 31-300 4.49e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 50.71  E-value: 4.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  31 ADKLPLVIAHGGPGCTHDYVDSFKDIAAtGRPVIHYDQIGNGNSTRLPEKGaefwTVDFFLGELDALLDHLGIrDRYALL 110
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALAA-GRPVIALDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGI-ERAHLV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 111 GQSWGGMLGAEHAVLQPRGLKALVIAnSPASMklwGEgaaRLRADLPEDVQEALNRHEaagttsdpeyIKAqdvfyarHV 190
Cdd:PRK14875  203 GHSMGGAVALRLAARAPQRVASLTLI-APAGL---GP---EINGDYIDGFVAAESRRE----------LKP-------VL 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 191 CRIVPNPPEVQRTfdiMAKDSTVYNAMNGPNE---------FHvvGTMKTWTVIDRLDRIKVPVLAYRGHYDEateacVQ 261
Cdd:PRK14875  259 ELLFADPALVTRQ---MVEDLLKYKRLDGVDDalraladalFA--GGRQRVDLRDRLASLAIPVLVIWGEQDR-----II 328

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1755817234 262 PF---LDLIPDVRGHVFPNSAHMPHVEERADCMAVTEAFLAQ 300
Cdd:PRK14875  329 PAahaQGLPDGVAVHVLPGAGHMPQMEAAADVNRLLAEFLGK 370
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
23-167 1.32e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.47  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  23 YRITGDL----GADKLPLVI-AHGGPGCTHD-YVDSFKDIAATGRPVIHYDQIGNGNSTRLPEKGAEFWTVDFflgeLDA 96
Cdd:COG1506     8 TTLPGWLylpaDGKKYPVVVyVHGGPGSRDDsFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA----IDY 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1755817234  97 LLDHLGI-RDRYALLGQSWGGMLGAEHAVLQPRGLKALVIANSPASMKLWGEGAARLRA---DLPEDVQEALNRH 167
Cdd:COG1506    84 LAARPYVdPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTErlmGGPWEDPEAYAAR 158
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 36-288 2.62e-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: 44.39  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  36 LVIAHGGPGCthdyVDSFKDIAATGRPVIHYDQIGNGNSTRLPEkgaefwtvDF-FLGELDALLDHLGIRDRYALLGQSW 114
Cdd:pfam12697   1 VVLVHGAGLS----AAPLAALLAAGVAVLAPDLPGHGSSSPPPL--------DLaDLADLAALLDELGAARPVVLVGHSL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 115 GGMLGAEHAvlqPRGLKALVIANSPASMKLWGEGAARLRADLPEDVqealnrheaagttSDPEYIKAQdvFYARHVCRIV 194
Cdd:pfam12697  69 GGAVALAAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAAL-------------AAPAWLAAE--SLARGFLDDL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 195 PNPPEVQRTFDIMAKdstvynamngpnefhvVGTMKTWTVIDRLDRIKVPVLaYRGHYDEATEACVQPFLDLIPDVRGHV 274
Cdd:pfam12697 131 PADAEWAAALARLAA----------------LLAALALLPLAAWRDLPVPVL-VLAEEDRLVPELAQRLLAALAGARLVV 193

                         250
                  ....*....|....
gi 1755817234 275 FPNSAHMPHVEERA 288
Cdd:pfam12697 194 LPGAGHLPLDDPEE 207
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
 31-137 1.95e-04

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 42.26  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  31 ADKLPLVIAHGGPGCTHDYVDSFKDIAATGRPVIHYDQIGNGNSTRlPEKGAEFwTVDFFLGELDALLDHLGIRDRYaLL 110
Cdd:PRK00870   44 ADGPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDK-PTRREDY-TYARHVEWMRSWFEQLDLTDVT-LV 120

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1755817234 111 GQSWGGMLG----AEHavlqPRGLKALVIAN 137
Cdd:PRK00870  121 CQDWGGLIGlrlaAEH----PDRFARLVVAN 147
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
105-289 2.82e-04

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 41.54  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 105 DRYALLGQSWGGMLGAEHAVLQPRGLKALV-IANSP--ASMKLW----GEGAARLRADLPEDVQEALNRHEAAGTTSDPe 177
Cdd:PRK10349   74 DKAIWLGWSLGGLVASQIALTHPERVQALVtVASSPcfSARDEWpgikPDVLAGFQQQLSDDFQRTVERFLALQTMGTE- 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234 178 yIKAQDVFYARHVCRIVPNpPEVqrtfdimakdstvyNAMNGPNEFhvvgtMKTWTVIDRLDRIKVPVLAYRGHYDEATE 257
Cdd:PRK10349  153 -TARQDARALKKTVLALPM-PEV--------------DVLNGGLEI-----LKTVDLRQPLQNVSMPFLRLYGYLDGLVP 211

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1755817234 258 ACVQPFLD-LIPDVRGHVFPNSAHMPHVEERAD 289
Cdd:PRK10349  212 RKVVPMLDkLWPHSESYIFAKAAHAPFISHPAE 244
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 9-154 9.62e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 40.28  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234   9 VTEGVSPYRGYETWYR-----------ITGDLGADKLPLVIAHGGPGCTHDYVDSFKDIAATGRpVIHYDQIGNGNSTRL 77
Cdd:PLN02894   70 VNIGSGPPGSKVRWFRsasneprfintVTFDSKEDAPTLVMVHGYGASQGFFFRNFDALASRFR-VIAIDQLGWGGSSRP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  78 P--EKGAEfWTVDFFLGELDALLDHLGIRDrYALLGQSWGGMLGAEHAVLQPRGLKALVI---ANSPASMKLWGEGAARL 152
Cdd:PLN02894  149 DftCKSTE-ETEAWFIDSFEEWRKAKNLSN-FILLGHSFGGYVAAKYALKHPEHVQHLILvgpAGFSSESDDKSEWLTKF 226


                  ..
gi 1755817234 153 RA 154
Cdd:PLN02894  227 RA 228
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 35-185 1.04e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 39.98  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  35 PLVIAHGGPGCTHDYVDSFKDIAATGRpVIHYDQIGNGNSTRLPEkgaeFWTVDFFLGELDALLDHLGIRDRYaLLGQSW 114
Cdd:PRK03592   29 PIVFLHGNPTSSYLWRNIIPHLAGLGR-CLAPDLIGMGASDKPDI----DYTFADHARYLDAWFDALGLDDVV-LVGHDW 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1755817234 115 GGMLGAEHAVLQPRGLKALVIANSPASMKLWgegaarlrADLPEDVQE---ALnRHEAAGttsdPEYIKAQDVF 185
Cdd:PRK03592  103 GSALGFDWAARHPDRVRGIAFMEAIVRPMTW--------DDFPPAVRElfqAL-RSPGEG----EEMVLEENVF 163
PRK08775 PRK08775
homoserine O-succinyltransferase;
96-136 2.28e-03

homoserine O-succinyltransferase;


Pssm-ID: 181553 [Multi-domain]  Cd Length: 343  Bit Score: 39.00  E-value: 2.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1755817234  96 ALLDHLGIRDRYALLGQSWGGMLGAEHAVLQPRGLKALVIA 136
Cdd:PRK08775  129 LLLDALGIARLHAFVGYSYGALVGLQFASRHPARVRTLVVV 169
metX PRK00175
homoserine O-acetyltransferase; Provisional
 96-139 2.53e-03

homoserine O-acetyltransferase; Provisional


Pssm-ID: 234678 [Multi-domain]  Cd Length: 379  Bit Score: 39.02  E-value: 2.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1755817234  96 ALLDHLGIRDRYALLGQSWGGMLGAEHAVLQP-RGLKALVIANSP 139
Cdd:PRK00175  138 RLLDALGITRLAAVVGGSMGGMQALEWAIDYPdRVRSALVIASSA 182
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
 35-138 4.16e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 38.30  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1755817234  35 PLVIAHGGPGCTHDYV-------DSFKDIAAtgrpvihyDQIGNGNSTRLPEKGaefWTVDFFLGELDALLDHLGIrDRY 107
Cdd:PRK03204   36 PILLCHGNPTWSFLYRdiivalrDRFRCVAP--------DYLGFGLSERPSGFG---YQIDEHARVIGEFVDHLGL-DRY 103

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1755817234 108 ALLGQSWGGMLGAEHAVLQPRGLKALVIANS 138
Cdd:PRK03204  104 LSMGQDWGGPISMAVAVERADRVRGVVLGNT 134
 
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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