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Conserved domains on  [gi|985331726|gb|KXA15267|]
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BAAT/acyl-CoA thioester hydrolase protein [Gardnerella pickettii]

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, ...
130-341 7.73e-17

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 pfam08840:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 211  Bit Score: 78.09  E-value: 7.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  130 IPLEQFDDVINYINKNIKDNKP-ISVLGASKGAEYALNLACKYPEIDNLILISPSSYNFAGLDFkdygsswtYKGEQLPY 208
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPgIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLV--------YKDNPLPP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  209 IDIKKSSFSSFLKNIIVPTIIKSPISYKETyesaieqdsssQEKLIPVKNVKANILMMAGEDDLMWDSFAMAKKIKEQ-- 286
Cdd:pfam08840  73 LGEGMRRIKVNKDGLLDIRDMFNDPLSKPD-----------PKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERlq 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985331726  287 ----NPNAKIYSYKGAGHIF----------AGNGVLNLgriRIATGGTIESNDKARSESRKTIDAFLKE 341
Cdd:pfam08840 142 khgkEVEVQLVCYPGAGHLIeppyfphcgaSFHALVGM---PVLWGGEPKAHAKAQEDAWKKIQAFFHK 207
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
130-341 7.73e-17

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 78.09  E-value: 7.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  130 IPLEQFDDVINYINKNIKDNKP-ISVLGASKGAEYALNLACKYPEIDNLILISPSSYNFAGLDFkdygsswtYKGEQLPY 208
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPgIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLV--------YKDNPLPP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  209 IDIKKSSFSSFLKNIIVPTIIKSPISYKETyesaieqdsssQEKLIPVKNVKANILMMAGEDDLMWDSFAMAKKIKEQ-- 286
Cdd:pfam08840  73 LGEGMRRIKVNKDGLLDIRDMFNDPLSKPD-----------PKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERlq 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985331726  287 ----NPNAKIYSYKGAGHIF----------AGNGVLNLgriRIATGGTIESNDKARSESRKTIDAFLKE 341
Cdd:pfam08840 142 khgkEVEVQLVCYPGAGHLIeppyfphcgaSFHALVGM---PVLWGGEPKAHAKAQEDAWKKIQAFFHK 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-306 1.42e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.42  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  63 VTYVDEGRMQGFRFVPKEKSHKGLVICFGGSEGS---PNFENAKILAKEGYETFALFMFGMKNQESTLTKIPLEQFDDVI 139
Cdd:COG1506    2 FKSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSrddSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 140 NY-INKNIKDNKPISVLGASKGAEYALNLACKYPE-IDNLILISPSSynfaglDFKDYGSSWTYKGEQLpyidikkssfs 217
Cdd:COG1506   82 DYlAARPYVDPDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVS------DLRSYYGTTREYTERL----------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 218 sflkniivptiIKSPISYKETYE--SAIEQdsssqeklipVKNVKANILMMAGEDDLMW---DSFAMAKKIKEQNPNAKI 292
Cdd:COG1506  145 -----------MGGPWEDPEAYAarSPLAY----------ADKLKTPLLLIHGEADDRVppeQAERLYEALKKAGKPVEL 203
                        250
                 ....*....|....
gi 985331726 293 YSYKGAGHIFAGNG 306
Cdd:COG1506  204 LVYPGEGHGFSGAG 217
PHA02857 PHA02857
monoglyceride lipase; Provisional
137-300 6.47e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.02  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 137 DVINYIN--KNIKDNKPISVLGASKGAEYALNLACKYPEI-DNLILISPssynfagldfkdygsswTYKGEQLPYIDIKK 213
Cdd:PHA02857  82 DVVQHVVtiKSTYPGVPVFLLGHSMGATISILAAYKNPNLfTAMILMSP-----------------LVNAEAVPRLNLLA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 214 ssfsSFLKNIIVPTIIKSPIS-----------YKETYESAIEQD-------------SSSQEKLIPvkNVKANILMMAGE 269
Cdd:PHA02857 145 ----AKLMGIFYPNKIVGKLCpesvsrdmdevYKYQYDPLVNHEkikagfasqvlkaTNKVRKIIP--KIKTPILILQGT 218
                        170       180       190
                 ....*....|....*....|....*....|.
gi 985331726 270 DDLMWDSFAMAKKIKEQNPNAKIYSYKGAGH 300
Cdd:PHA02857 219 NNEISDVSGAYYFMQHANCNREIKIYEGAKH 249
 
Name Accession Description Interval E-value
BAAT_C pfam08840
BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C ...
130-341 7.73e-17

BAAT / Acyl-CoA thioester hydrolase C terminal; This catalytic domain is found at the C terminal of acyl-CoA thioester hydrolases and bile acid-CoA:amino acid N-acetyltransferases (BAAT).


Pssm-ID: 430252 [Multi-domain]  Cd Length: 211  Bit Score: 78.09  E-value: 7.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  130 IPLEQFDDVINYINKNIKDNKP-ISVLGASKGAEYALNLACKYPEIDNLILISPSSYNFAGLDFkdygsswtYKGEQLPY 208
Cdd:pfam08840   1 VDLEYFEEAINYLLRHPKVKGPgIGLLGISKGGELALSMATFLKQITATVSINGSAVVSGDPLV--------YKDNPLPP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  209 IDIKKSSFSSFLKNIIVPTIIKSPISYKETyesaieqdsssQEKLIPVKNVKANILMMAGEDDLMWDSFAMAKKIKEQ-- 286
Cdd:pfam08840  73 LGEGMRRIKVNKDGLLDIRDMFNDPLSKPD-----------PKSLIPVERAKGPFLFVVGQDDHNWPSVFYAKKACERlq 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 985331726  287 ----NPNAKIYSYKGAGHIF----------AGNGVLNLgriRIATGGTIESNDKARSESRKTIDAFLKE 341
Cdd:pfam08840 142 khgkEVEVQLVCYPGAGHLIeppyfphcgaSFHALVGM---PVLWGGEPKAHAKAQEDAWKKIQAFFHK 207
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
63-306 1.42e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.42  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  63 VTYVDEGRMQGFRFVPKEKSHKGLVICFGGSEGS---PNFENAKILAKEGYETFALFMFGMKNQESTLTKIPLEQFDDVI 139
Cdd:COG1506    2 FKSADGTTLPGWLYLPADGKKYPVVVYVHGGPGSrddSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 140 NY-INKNIKDNKPISVLGASKGAEYALNLACKYPE-IDNLILISPSSynfaglDFKDYGSSWTYKGEQLpyidikkssfs 217
Cdd:COG1506   82 DYlAARPYVDPDRIGIYGHSYGGYMALLAAARHPDrFKAAVALAGVS------DLRSYYGTTREYTERL----------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 218 sflkniivptiIKSPISYKETYE--SAIEQdsssqeklipVKNVKANILMMAGEDDLMW---DSFAMAKKIKEQNPNAKI 292
Cdd:COG1506  145 -----------MGGPWEDPEAYAarSPLAY----------ADKLKTPLLLIHGEADDRVppeQAERLYEALKKAGKPVEL 203
                        250
                 ....*....|....
gi 985331726 293 YSYKGAGHIFAGNG 306
Cdd:COG1506  204 LVYPGEGHGFSGAG 217
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
62-342 4.84e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 59.16  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  62 DVTYV--DEGRMQGFRFVPK--EKSHKGLVIC--FGGS-EGSPNFenAKILAKEGyetFALFMFGMKNQ-EST---LTKI 130
Cdd:COG1073   12 DVTFKsrDGIKLAGDLYLPAgaSKKYPAVVVAhgNGGVkEQRALY--AQRLAELG---FNVLAFDYRGYgESEgepREEG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 131 PLEQFD--DVINYINKNIK-DNKPISVLGASKGAEYALNLACKYPEIDNLILISPssYNfaglDFKDYGSSWT--YKGEQ 205
Cdd:COG1073   87 SPERRDarAAVDYLRTLPGvDPERIGLLGISLGGGYALNAAATDPRVKAVILDSP--FT----SLEDLAAQRAkeARGAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 206 LPYIdikkssfsSFLKNIIVPTIIKSPIsyketyeSAIEQdsssqeklipVKNVKANILMMAGEDDLMwDSFAMAKKIKE 285
Cdd:COG1073  161 LPGV--------PYLPNVRLASLLNDEF-------DPLAK----------IEKISRPLLFIHGEKDEA-VPFYMSEDLYE 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 985331726 286 QNPNAK-IYSYKGAGHifagngvlnlgririatggtIESNDKARSESRKTIDAFLKEN 342
Cdd:COG1073  215 AAAEPKeLLIVPGAGH--------------------VDLYDRPEEEYFDKLAEFFKKN 252
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
86-302 3.53e-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: 56.74  E-value: 3.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726   86 LVICFGGSEGSPNFEN-AKILAKEGYETFALFMFGMkNQESTLTKIPLEQFDDVINYINK--NIKDNKPISVLGASKGAE 162
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKlAPALARDGFRVIALDLRGF-GKSSRPKAQDDYRTDDLAEDLEYilEALGLEKVNLVGHSMGGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  163 YALNLACKYPE-IDNLILISPSSYNFAGLDFKDYGSSWTYKGEQLPYIDIKKSSFSSFLKNIIV---------------- 225
Cdd:pfam00561  82 IALAYAAKYPDrVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLLAllllrlrllkalplln 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  226 -------PTIIKSPISYKETYESAIEQDSSSQEKLIPVKNVkaniLMMAGEDDLMWDSFAMAkKIKEQNPNAKIYSYKGA 298
Cdd:pfam00561 162 krfpsgdYALAKSLVTGALLFIETWSTELRAKFLGRLDEPT----LIIWGDQDPLVPPQALE-KLAQLFPNARLVVIPDA 236

                  ....
gi 985331726  299 GHIF 302
Cdd:pfam00561 237 GHFA 240
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
61-340 9.71e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 54.97  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726  61 VDVTYVDEGRMQGFRFVPKEKSHKGLVI----CFGGSEgsPNFENAKILAKEGYETFALFMFG-----------MKNQES 125
Cdd:COG0412    6 VTIPTPDGVTLPGYLARPAGGGPRPGVVvlheIFGLNP--HIRDVARRLAAAGYVVLAPDLYGrggpgddpdeaRALMGA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 126 TLTKIPLEQFDDVINYINKN-IKDNKPISVLGASKGAEYALNLACKYPEIDnlilispssynfAGLDFkdYGSSWTYKGE 204
Cdd:COG0412   84 LDPELLAADLRAALDWLKAQpEVDAGRVGVVGFCFGGGLALLAAARGPDLA------------AAVSF--YGGLPADDLL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 205 QLpyidikkssfssflkniivptiikspisyketyesaieqdsssqeklipVKNVKANILMMAGEDDLMW---DSFAMAK 281
Cdd:COG0412  150 DL-------------------------------------------------AARIKAPVLLLYGEKDPLVppeQVAALEA 180
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 985331726 282 KIKEQNPNAKIYSYKGAGHIFAgngvlNLGRIRiatggtieSNDKARSESRKTIDAFLK 340
Cdd:COG0412  181 ALAAAGVDVELHVYPGAGHGFT-----NPGRPR--------YDPAAAEDAWQRTLAFLA 226
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
102-303 3.56e-06

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 47.63  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 102 AKILAKEGYETFALFMFGMKNQESTLTKIPLEQF-DDVINYINKNIKDNKPISVLGASKGAEYALNLACKYPEIDNLILI 180
Cdd:COG1647   35 AEALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWlEDVEEAYEILKAGYDKVIVIGLSMGGLLALLLAARYPDVAGLVLL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 181 SPssynfagldfkdygsSWTYKGEQLPYIDIKKsSFSSFLKNIivPTIIKSPISYKETYE-----SAIEQDSSSQEKLIP 255
Cdd:COG1647  115 SP---------------ALKIDDPSAPLLPLLK-YLARSLRGI--GSDIEDPEVAEYAYDrtplrALAELQRLIREVRRD 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 985331726 256 VKNVKANILMMAGEDDLM---WDSFAMAKKIKeqNPNAKIYSYKGAGHIFA 303
Cdd:COG1647  177 LPKITAPTLIIQSRKDEVvppESARYIYERLG--SPDKELVWLEDSGHVIT 225
PHA02857 PHA02857
monoglyceride lipase; Provisional
137-300 6.47e-04

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 41.02  E-value: 6.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 137 DVINYIN--KNIKDNKPISVLGASKGAEYALNLACKYPEI-DNLILISPssynfagldfkdygsswTYKGEQLPYIDIKK 213
Cdd:PHA02857  82 DVVQHVVtiKSTYPGVPVFLLGHSMGATISILAAYKNPNLfTAMILMSP-----------------LVNAEAVPRLNLLA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726 214 ssfsSFLKNIIVPTIIKSPIS-----------YKETYESAIEQD-------------SSSQEKLIPvkNVKANILMMAGE 269
Cdd:PHA02857 145 ----AKLMGIFYPNKIVGKLCpesvsrdmdevYKYQYDPLVNHEkikagfasqvlkaTNKVRKIIP--KIKTPILILQGT 218
                        170       180       190
                 ....*....|....*....|....*....|.
gi 985331726 270 DDLMWDSFAMAKKIKEQNPNAKIYSYKGAGH 300
Cdd:PHA02857 219 NNEISDVSGAYYFMQHANCNREIKIYEGAKH 249
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
82-182 8.17e-03

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: 37.19  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331726   82 SHKGLV-ICFGGSEGSPNFEN-AKILAKEGYETFALFMFGMKNQESTLTKIP-LEQF-DDVINYINKNIKD--NKPISVL 155
Cdd:pfam12146   2 EPRAVVvLVHGLGEHSGRYAHlADALAAQGFAVYAYDHRGHGRSDGKRGHVPsFDDYvDDLDTFVDKIREEhpGLPLFLL 81
                          90       100
                  ....*....|....*....|....*...
gi 985331726  156 GASKGAEYALNLACKYPE-IDNLILISP 182
Cdd:pfam12146  82 GHSMGGLIAALYALRYPDkVDGLILSAP 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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