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Conserved domains on  [gi|2674045002|ref|WP_331645372|]
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alpha/beta fold hydrolase [Luteibacter sp.]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11455169)

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
PubMed:  37582413|12369917|19508187

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
66-287 1.04e-21

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


:

Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  66 MTARRDSVE-VNGEQIATYVWG-DPATQPYILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDFV 143
Cdd:COG2267     1 MTRRLVTLPtRDGLRLRGRRWRpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 144 RTVT-------VIGRHYGDAEGVIAHSLGGA-AVTLALDHGWTAKRVVLIAPA--ADPEAATSrfARFVRlaahlrpslh 213
Cdd:COG2267    81 DYVDdlraaldALRARPGLPVVLLGHSMGGLiALLYAARYPDRVAGLVLLAPAyrADPLLGPS--ARWLR---------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674045002 214 dtltartgvaigDLHIRHHAPKRTQPALIVHDVSDRDVPVGEGE-LYATLWPGATLLKTRDLGHRRIVDDEHVQA 287
Cdd:COG2267   149 ------------ALRLAEALARIDVPVLVLHGGADRVVPPEAARrLAARLSPDVELVLLPGARHELLNEPAREEV 211
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
66-287 1.04e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  66 MTARRDSVE-VNGEQIATYVWG-DPATQPYILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDFV 143
Cdd:COG2267     1 MTRRLVTLPtRDGLRLRGRRWRpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 144 RTVT-------VIGRHYGDAEGVIAHSLGGA-AVTLALDHGWTAKRVVLIAPA--ADPEAATSrfARFVRlaahlrpslh 213
Cdd:COG2267    81 DYVDdlraaldALRARPGLPVVLLGHSMGGLiALLYAARYPDRVAGLVLLAPAyrADPLLGPS--ARWLR---------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674045002 214 dtltartgvaigDLHIRHHAPKRTQPALIVHDVSDRDVPVGEGE-LYATLWPGATLLKTRDLGHRRIVDDEHVQA 287
Cdd:COG2267   149 ------------ALRLAEALARIDVPVLVLHGGADRVVPPEAARrLAARLSPDVELVLLPGARHELLNEPAREEV 211
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 94-252 3.23e-11

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: 61.85  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  94 ILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDF------VRTV--TVIGRHYGDAEGVIAHSLG 165
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFddyvddLDTFvdKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 166 GAAVTL-ALDHGWTAKRVVLIAPA-ADPEAATSRFARFV-RLAAHLRPSL---------------------------HDT 215
Cdd:pfam12146  87 GLIAALyALRYPDKVDGLILSAPAlKIKPYLAPPILKLLaKLLGKLFPRLrvpnnllpdslsrdpevvaayaadplvHGG 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674045002 216 LTARTGVAIGDL--HIRHHAPKRTQPALIVHDVSDRDVP 252
Cdd:pfam12146 167 ISARTLYELLDAgeRLLRRAAAITVPLLLLHGGADRVVD 205
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 44-188 2.31e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.24  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  44 AARVFQTPLASSRERAVHALATMTARRDSVEVNGEQIATYVWGDPATQPyILLVHGWSSLGlrwESWAAQL--LAKGWAA 121
Cdd:PRK14875   85 EIDAFIAPFARRFAPEGIDEEDAGPAPRKARIGGRTVRYLRLGEGDGTP-VVLIHGFGGDL---NNWLFNHaaLAAGRPV 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674045002 122 VAFDQPAHGHSGGELC--TLPDFVRTVTVIGRHYG-DAEGVIAHSLGGA-AVTLALDHGWTAKRVVLIAPA 188
Cdd:PRK14875  161 IALDLPGHGASSKAVGagSLDELAAAVLAFLDALGiERAHLVGHSMGGAvALRLAARAPQRVASLTLIAPA 231
 
Name Accession Description Interval E-value
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
66-287 1.04e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 90.83  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  66 MTARRDSVE-VNGEQIATYVWG-DPATQPYILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDFV 143
Cdd:COG2267     1 MTRRLVTLPtRDGLRLRGRRWRpAGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 144 RTVT-------VIGRHYGDAEGVIAHSLGGA-AVTLALDHGWTAKRVVLIAPA--ADPEAATSrfARFVRlaahlrpslh 213
Cdd:COG2267    81 DYVDdlraaldALRARPGLPVVLLGHSMGGLiALLYAARYPDRVAGLVLLAPAyrADPLLGPS--ARWLR---------- 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2674045002 214 dtltartgvaigDLHIRHHAPKRTQPALIVHDVSDRDVPVGEGE-LYATLWPGATLLKTRDLGHRRIVDDEHVQA 287
Cdd:COG2267   149 ------------ALRLAEALARIDVPVLVLHGGADRVVPPEAARrLAARLSPDVELVLLPGARHELLNEPAREEV 211
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 66-276 3.52e-19

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: 83.90  E-value: 3.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  66 MTARRdSVEVNGEQIATYVWGDPAtqPYILLVHGWSSLGLRWESWAAqLLAKGWAAVAFDQPAHGHSGG--ELCTLPDFV 143
Cdd:COG0596     1 MSTPR-FVTVDGVRLHYREAGPDG--PPVVLLHGLPGSSYEWRPLIP-ALAAGYRVIAPDLRGHGRSDKpaGGYTLDDLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 144 RTVTVIGRHYGDAE-GVIAHSLGGA-AVTLALDHGWTAKRVVLIAPAADpeaatsRFARFVRLAAHLRPSLHDTLTARTG 221
Cdd:COG0596    77 DDLAALLDALGLERvVLVGHSMGGMvALELAARHPERVAGLVLVDEVLA------ALAEPLRRPGLAPEALAALLRALAR 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2674045002 222 VAIgdlhiRHHAPKRTQPALIVHDVSDRDVPVGEGELYATLWPGATLLKTRDLGH 276
Cdd:COG0596   151 TDL-----RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGH 200
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
76-262 1.97e-14

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 71.20  E-value: 1.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  76 NGEQIATYVWGDPATQPY--ILLVHGW-SSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCT--LPDFVRTVT-VI 149
Cdd:COG1506     6 DGTTLPGWLYLPADGKKYpvVVYVHGGpGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGdeVDDVLAAIDyLA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 150 GRHYGDAE--GVIAHSLGGAAVTLAL-DHGWTAKRVVLIAPAADPEAATSRFARFVRLAAHLRPSLHDTLTARTGVaigd 226
Cdd:COG1506    86 ARPYVDPDriGIYGHSYGGYMALLAAaRHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAARSPL---- 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2674045002 227 lhirHHAPKRTQPALIVHDVSDRDVPVGEGE-LYATL 262
Cdd:COG1506   162 ----AYADKLKTPLLLIHGEADDRVPPEQAErLYEAL 194
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
94-253 8.51e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 63.81  E-value: 8.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  94 ILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGEL--CTLPDFVRTVT---VIGRHYGDAEGVIAHSLGGA- 167
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLlkTTWEDWLEDVEeayEILKAGYDKVIVIGLSMGGLl 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 168 AVTLALDHGwTAKRVVLIAPAADPEaatSRFARFVRLAAHLRPSLH----------------DTLTARTGVAIGDL--HI 229
Cdd:COG1647    98 ALLLAARYP-DVAGLVLLSPALKID---DPSAPLLPLLKYLARSLRgigsdiedpevaeyayDRTPLRALAELQRLirEV 173

                         170       180
                  ....*....|....*....|....
gi 2674045002 230 RHHAPKRTQPALIVHDVSDRDVPV 253
Cdd:COG1647   174 RRDLPKITAPTLIIQSRKDEVVPP 197
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 94-252 3.23e-11

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: 61.85  E-value: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  94 ILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDF------VRTV--TVIGRHYGDAEGVIAHSLG 165
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFddyvddLDTFvdKIREEHPGLPLFLLGHSMG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 166 GAAVTL-ALDHGWTAKRVVLIAPA-ADPEAATSRFARFV-RLAAHLRPSL---------------------------HDT 215
Cdd:pfam12146  87 GLIAALyALRYPDKVDGLILSAPAlKIKPYLAPPILKLLaKLLGKLFPRLrvpnnllpdslsrdpevvaayaadplvHGG 166

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2674045002 216 LTARTGVAIGDL--HIRHHAPKRTQPALIVHDVSDRDVP 252
Cdd:pfam12146 167 ISARTLYELLDAgeRLLRRAAAITVPLLLLHGGADRVVD 205
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 76-260 1.48e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 60.31  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  76 NGEQIATYVW---GDPATQPYILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGE-----LCTLPDFVRTVT 147
Cdd:COG1073    19 DGIKLAGDLYlpaGASKKYPAVVVAHGNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESEGEpreegSPERRDARAAVD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002 148 VIGRH-YGDAE--GVIAHSLGGA-AVTLALDHGwTAKRVVLIAPAAD-PEAATSRFARFVRL---AAHLRPSLHDTLTAR 219
Cdd:COG1073    99 YLRTLpGVDPEriGLLGISLGGGyALNAAATDP-RVKAVILDSPFTSlEDLAAQRAKEARGAylpGVPYLPNVRLASLLN 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2674045002 220 TGVAigdlhIRHHAPKRTQPALIVHdvSDRD--VPVGEGE-LYA 260
Cdd:COG1073   178 DEFD-----PLAKIEKISRPLLFIH--GEKDeaVPFYMSEdLYE 214
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 94-203 1.29e-08

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: 54.43  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  94 ILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELC----TLPDFVRTVTVIGRHYGDAE-GVIAHSLGGA- 167
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAqddyRTDDLAEDLEYILEALGLEKvNLVGHSMGGLi 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2674045002 168 AVTLALDHGWTAKRVVLIAPAADPeAATSRFARFVR 203
Cdd:pfam00561  83 ALAYAAKYPDRVKALVLLGALDPP-HELDEADRFIL 117
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 94-241 4.21e-06

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 46.70  E-value: 4.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  94 ILLVHGWSSLGLRWeswaAQLLAKGWAAVAFDQPAHGHSGGELCTLPDFVRTVTVIGRHYGDAEGV-IAHSLGGAAVTLA 172
Cdd:pfam12697   1 VVLVHGAGLSAAPL----AALLAAGVAVLAPDLPGHGSSSPPPLDLADLADLAALLDELGAARPVVlVGHSLGGAVALAA 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2674045002 173 LDHGwTAKRVVLIAPAADPEAATSRFARFVRLAAHLRPSLHDTLTARTGVAIGDLHIRHHAPKRTQPAL 241
Cdd:pfam12697  77 AAAA-LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLA 144
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 89-187 7.19e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 44.05  E-value: 7.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  89 ATQPYILLVHGWSSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGEL-CTLPDFVRTVTvigRHYGDAE-GVIAHSLGG 166
Cdd:COG1075     3 ATRYPVVLVHGLGGSAASWAPLAPRLRAAGYPVYALNYPSTNGSIEDSaEQLAAFVDAVL---AATGAEKvDLVGHSMGG 79

                          90       100
                  ....*....|....*....|....
gi 2674045002 167 AAVTLAL-DHGWTAK--RVVLIAP 187
Cdd:COG1075    80 LVARYYLkRLGGAAKvaRVVTLGT 103
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 44-188 2.31e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 42.24  E-value: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  44 AARVFQTPLASSRERAVHALATMTARRDSVEVNGEQIATYVWGDPATQPyILLVHGWSSLGlrwESWAAQL--LAKGWAA 121
Cdd:PRK14875   85 EIDAFIAPFARRFAPEGIDEEDAGPAPRKARIGGRTVRYLRLGEGDGTP-VVLIHGFGGDL---NNWLFNHaaLAAGRPV 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2674045002 122 VAFDQPAHGHSGGELC--TLPDFVRTVTVIGRHYG-DAEGVIAHSLGGA-AVTLALDHGWTAKRVVLIAPA 188
Cdd:PRK14875  161 IALDLPGHGASSKAVGagSLDELAAAVLAFLDALGiERAHLVGHSMGGAvALRLAARAPQRVASLTLIAPA 231
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 70-187 8.43e-04

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 40.51  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  70 RDSVEVN--GEQIATYVWGDPATQP--YILLVHGW-SSLGLRWESWAAQLLAKGWAAVAFDQPAHGHSGGELCTLPDFVR 144
Cdd:PLN02385   62 EESYEVNsrGVEIFSKSWLPENSRPkaAVCFCHGYgDTCTFFFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFDD 141

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2674045002 145 TVTVIGRHYGDAEG----------VIAHSLGGaAVTLALD----HGWTAkrVVLIAP 187
Cdd:PLN02385  142 LVDDVIEHYSKIKGnpefrglpsfLFGQSMGG-AVALKVHlkqpNAWDG--AILVAP 195
PRK05855 PRK05855
SDR family oxidoreductase;
66-133 8.57e-04

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 40.73  E-value: 8.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2674045002  66 MTARRDSVEVNGEQIATYVWGDPAtQPYILLVHGWSSLGLRWESWAAqLLAKGWAAVAFDQPAHGHSG 133
Cdd:PRK05855    1 SQPRRTVVSSDGVRLAVYEWGDPD-RPTVVLVHGYPDNHEVWDGVAP-LLADRFRVVAYDVRGAGRSS 66
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
76-200 9.56e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2674045002  76 NGEQIATYVWGDPATQPY--ILLVHGWSSLGLRWESWAAQLLAKGWAAVAFD------QPAHGHSGGEL-------CTLP 140
Cdd:COG0412    12 DGVTLPGYLARPAGGGPRpgVVVLHEIFGLNPHIRDVARRLAAAGYVVLAPDlygrggPGDDPDEARALmgaldpeLLAA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2674045002 141 DFVRTVTVIGRH-YGDAE--GVIAHSLGGAAVTLALDHGWTAKRVVLIAPAADPEAATSRFAR 200
Cdd:COG0412    92 DLRAALDWLKAQpEVDAGrvGVVGFCFGGGLALLAAARGPDLAAAVSFYGGLPADDLLDLAAR 154
 
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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