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Conserved domains on  [gi|488221597|ref|WP_002292805|]
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MULTISPECIES: alpha/beta hydrolase [Enterococcus]

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

 Zoom to residue level

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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]; ...
78-317 6.31e-55

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


:

Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 179.34  E-value: 6.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFI--QPTQQNKWVICVHDYRSTgKRDMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDRLD 155
Cdd:COG1073   14 TFKSRDGIKLAGDLYLpaGASKKYPAVVVAHGNGGV-KEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERRD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 156 LIAWIQLI--LDEQPDASIILHGGSMGASTIMMASGEkLPsAVKGFILDSGYVSVYAEFRYMLSKitvFPKKMIMRYANH 233
Cdd:COG1073   93 ARAAVDYLrtLPGVDPERIGLLGISLGGGYALNAAAT-DP-RVKAVILDSPFTSLEDLAAQRAKE---ARGAYLPGVPYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 234 YAQKYAGYSLKQASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNATAGDKALLLVPEAEHLEASMKDPKTYWTVIFS 313
Cdd:COG1073  168 PNVRLASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDKLAE 247

                 ....
gi 488221597 314 FIEQ 317
Cdd:COG1073  248 FFKK 251
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
78-317 6.31e-55

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 179.34  E-value: 6.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFI--QPTQQNKWVICVHDYRSTgKRDMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDRLD 155
Cdd:COG1073   14 TFKSRDGIKLAGDLYLpaGASKKYPAVVVAHGNGGV-KEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERRD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 156 LIAWIQLI--LDEQPDASIILHGGSMGASTIMMASGEkLPsAVKGFILDSGYVSVYAEFRYMLSKitvFPKKMIMRYANH 233
Cdd:COG1073   93 ARAAVDYLrtLPGVDPERIGLLGISLGGGYALNAAAT-DP-RVKAVILDSPFTSLEDLAAQRAKE---ARGAYLPGVPYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 234 YAQKYAGYSLKQASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNATAGDKALLLVPEAEHLEASMKDPKTYWTVIFS 313
Cdd:COG1073  168 PNVRLASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDKLAE 247

                 ....
gi 488221597 314 FIEQ 317
Cdd:COG1073  248 FFKK 251
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
97-296 3.21e-16

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: 76.48  E-value: 3.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597   97 QQNKWVIC-VHDYRSTGKRdMSHIGKRYAEKGFNVLIPDLRAHGESEGEIigmGWLDRL-----DLIAWIQLILDEQPDA 170
Cdd:pfam12146   1 GEPRAVVVlVHGLGEHSGR-YAHLADALAAQGFAVYAYDHRGHGRSDGKR---GHVPSFddyvdDLDTFVDKIREEHPGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  171 SIILHGGSMGAsTIMMASGEKLPSAVKGFILDSGYVSVYAEF--------RYMLSKitVFPKKMIM-RYANHYAQKY--- 238
Cdd:pfam12146  77 PLFLLGHSMGG-LIAALYALRYPDKVDGLILSAPALKIKPYLappilkllAKLLGK--LFPRLRVPnNLLPDSLSRDpev 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488221597  239 -----------------AGYSLKQAS--ATRQLGSNHLPLLVIHGERDHFVPTEAAYT-IQNATAGDKALLLVPEAEH 296
Cdd:pfam12146 154 vaayaadplvhggisarTLYELLDAGerLLRRAAAITVPLLLLHGGADRVVDPAGSREfYERAGSTDKTLKLYPGLYH 231
 
Name Accession Description Interval E-value
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
78-317 6.31e-55

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 179.34  E-value: 6.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFI--QPTQQNKWVICVHDYRSTgKRDMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDRLD 155
Cdd:COG1073   14 TFKSRDGIKLAGDLYLpaGASKKYPAVVVAHGNGGV-KEQRALYAQRLAELGFNVLAFDYRGYGESEGEPREEGSPERRD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 156 LIAWIQLI--LDEQPDASIILHGGSMGASTIMMASGEkLPsAVKGFILDSGYVSVYAEFRYMLSKitvFPKKMIMRYANH 233
Cdd:COG1073   93 ARAAVDYLrtLPGVDPERIGLLGISLGGGYALNAAAT-DP-RVKAVILDSPFTSLEDLAAQRAKE---ARGAYLPGVPYL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 234 YAQKYAGYSLKQASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNATAGDKALLLVPEAEHLEASMKDPKTYWTVIFS 313
Cdd:COG1073  168 PNVRLASLLNDEFDPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLYDRPEEEYFDKLAE 247

                 ....
gi 488221597 314 FIEQ 317
Cdd:COG1073  248 FFKK 251
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
78-319 6.84e-29

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 110.88  E-value: 6.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFI-QPTQQNKWVICVHDYRSTGKRDMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDRLDL 156
Cdd:COG1506    1 TFKSADGTTLPGWLYLpADGKKYPVVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 157 IAWiqliLDEQPDA---SIILHGGSMGASTIMMASGEKlPSAVKGFILDSGYVSvyaeFRYMLSKITVFPKkmimRYANH 233
Cdd:COG1506   81 IDY----LAARPYVdpdRIGIYGHSYGGYMALLAAARH-PDRFKAAVALAGVSD----LRSYYGTTREYTE----RLMGG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 234 YAQKYAGYslKQASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNA---TAGDKALLLVPEAEHLEASMKDPKtYWTV 310
Cdd:COG1506  148 PWEDPEAY--AARSPLAYADKLKTPLLLIHGEADDRVPPEQAERLYEAlkkAGKPVELLVYPGEGHGFSGAGAPD-YLER 224

                 ....*....
gi 488221597 311 IFSFIEQRI 319
Cdd:COG1506  225 ILDFLDRHL 233
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
78-317 6.56e-27

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 105.47  E-value: 6.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFIQPTQQNKWVICVHDYRSTGKRdMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDRL--D 155
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPRGTVVLVHGLGEHSGR-YAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYvdD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 156 LIAWIQLILdEQPDASIILHGGSMGAsTIMMASGEKLPSAVKGFILDSGyvsvyaefrymlskitvfpkkmimRYANHYA 235
Cdd:COG2267   86 LRAALDALR-ARPGLPVVLLGHSMGG-LIALLYAARYPDRVAGLVLLAP------------------------AYRADPL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 236 QKYAGYSLKQASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNATAGDKALLLVPEAEHLEASMKDPKTYWTVIFSFI 315
Cdd:COG2267  140 LGPSARWLRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNEPAREEVLAAILAWL 219

                 ..
gi 488221597 316 EQ 317
Cdd:COG2267  220 ER 221
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
102-317 5.17e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 92.70  E-value: 5.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 102 VICVHDYRSTgKRDMSHIGKRYAEKGFNVLIPDLRAHGESEGEIIGMGWLDrldliaWIQ------LILDEQPDaSIILH 175
Cdd:COG1647   18 VLLLHGFTGS-PAEMRPLAEALAKAGYTVYAPRLPGHGTSPEDLLKTTWED------WLEdveeayEILKAGYD-KVIVI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 176 GGSMGASTIMMASgEKLPsAVKGFILDSGYVSVY---AEFRYMLSKITVFPKKM--IMRYANHYAQKYAGYSLKQ----- 245
Cdd:COG1647   90 GLSMGGLLALLLA-ARYP-DVAGLVLLSPALKIDdpsAPLLPLLKYLARSLRGIgsDIEDPEVAEYAYDRTPLRAlaelq 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488221597 246 ---ASATRQLGSNHLPLLVIHGERDHFVPTEAAYTIQNATAG-DKALLLVPEAEHLEASMKDPKTYWTVIFSFIEQ 317
Cdd:COG1647  168 rliREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSpDKELVWLEDSGHVITLDKDREEVAEEILDFLER 243
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
97-296 3.21e-16

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: 76.48  E-value: 3.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597   97 QQNKWVIC-VHDYRSTGKRdMSHIGKRYAEKGFNVLIPDLRAHGESEGEIigmGWLDRL-----DLIAWIQLILDEQPDA 170
Cdd:pfam12146   1 GEPRAVVVlVHGLGEHSGR-YAHLADALAAQGFAVYAYDHRGHGRSDGKR---GHVPSFddyvdDLDTFVDKIREEHPGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  171 SIILHGGSMGAsTIMMASGEKLPSAVKGFILDSGYVSVYAEF--------RYMLSKitVFPKKMIM-RYANHYAQKY--- 238
Cdd:pfam12146  77 PLFLLGHSMGG-LIAALYALRYPDKVDGLILSAPALKIKPYLappilkllAKLLGK--LFPRLRVPnNLLPDSLSRDpev 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488221597  239 -----------------AGYSLKQAS--ATRQLGSNHLPLLVIHGERDHFVPTEAAYT-IQNATAGDKALLLVPEAEH 296
Cdd:pfam12146 154 vaayaadplvhggisarTLYELLDAGerLLRRAAAITVPLLLLHGGADRVVDPAGSREfYERAGSTDKTLKLYPGLYH 231
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
102-318 3.92e-14

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: 70.42  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 102 VICVHDYRSTGkRDMSHIGKRYAEkGFNVLIPDLRAHGESEGEIIGMGWLDrldLIAWIQLILDEQPDASIILHGGSMGA 181
Cdd:COG0596   26 VVLLHGLPGSS-YEWRPLIPALAA-GYRVIAPDLRGHGRSDKPAGGYTLDD---LADDLAALLDALGLERVVLVGHSMGG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 182 STIMMAsGEKLPSAVKGFILDSGYVSVYAEfryMLSKITVFPKKMIMRYAnhyaqkyagySLKQASATRQLGSNHLPLLV 261
Cdd:COG0596  101 MVALEL-AARHPERVAGLVLVDEVLAALAE---PLRRPGLAPEALAALLR----------ALARTDLRERLARITVPTLV 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488221597 262 IHGERDHFVPTEAAYTIQNATAGDKaLLLVPEAEHLeASMKDPKTYWTVIFSFIEQR 318
Cdd:COG0596  167 IWGEKDPIVPPALARRLAELLPNAE-LVVLPGAGHF-PPLEQPEAFAAALRDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
100-297 4.32e-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: 55.97  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  100 KWVICVHDYrsTGKRDMSHIGKRY-AEKGFNVLIPDLRAHGESEGEIigmgWLDR---LDLIAWIQLILDEQPDASIILH 175
Cdd:pfam00561   1 PPVLLLHGL--PGSSDLWRKLAPAlARDGFRVIALDLRGFGKSSRPK----AQDDyrtDDLAEDLEYILEALGLEKVNLV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  176 GGSMGaSTIMMASGEKLPSAVKGFILDSGYVSVYAE--------------FRYMLSKITVFP------------------ 223
Cdd:pfam00561  75 GHSMG-GLIALAYAAKYPDRVKALVLLGALDPPHELdeadrfilalfpgfFDGFVADFAPNPlgrlvakllallllrlrl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  224 ----KKMIMRYANHY---AQKYAGYSLKQASATRQLGSNHL------PLLVIHGERDHFVPTEAAYTIQNATaGDKALLL 290
Cdd:pfam00561 154 lkalPLLNKRFPSGDyalAKSLVTGALLFIETWSTELRAKFlgrldePTLIIWGDQDPLVPPQALEKLAQLF-PNARLVV 232

                  ....*..
gi 488221597  291 VPEAEHL 297
Cdd:pfam00561 233 IPDAGHF 239
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
121-297 6.35e-08

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


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 52.09  E-value: 6.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 121 KRYAEKGFNVLIPDLRAHGESEGEIiGMGWLDRLDL---IAWIQlildEQPDASIILHGGSMGASTIMMAsGEKLPsAVK 197
Cdd:COG2945   49 RALVAAGFAVLRFNFRGVGRSEGEF-DEGRGELDDAaaaLDWLR----AQNPLPLWLAGFSFGAYVALQL-AMRLP-EVE 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597 198 GFILdsgyVSVyAEFRYMLSKITVFPKkmimryanhyaqkyagyslkqasatrqlgsnhlPLLVIHGERDHFVPTEAAYT 277
Cdd:COG2945  122 GLIL----VAP-PVNRYDFSFLAPCPA---------------------------------PTLVIHGEQDEVVPPAEVLD 163
                        170       180
                 ....*....|....*....|
gi 488221597 278 IQNATAGDKALLLVPEAEHL 297
Cdd:COG2945  164 WARPLSPPLPVVVVPGADHF 183
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
78-201 2.13e-05

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 45.26  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  78 TIKSYDGLKLAGQMFIQPTQQNKWVICVHdyrSTGkrdmshIGKRY--------AEKGFNVLIPDLRAHGES---EGEII 146
Cdd:COG4757   11 TITAADGYPLAARLFPPAGPPRAVVLINP---ATG------VPQRFyrpfarylAERGFAVLTYDYRGIGLSrpgSLRGF 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488221597 147 GMGWLD--RLDLIAWIQLILDEQPDASIILHGGSMGASTIMMASGeklPSAVKGFIL 201
Cdd:COG4757   82 DAGYRDwgELDLPAVLDALRARFPGLPLLLVGHSLGGQLLGLAPN---AERVDRLVT 135
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
122-297 1.90e-04

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 42.08  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  122 RYAEKGFNVLIPDLRAHGESEGEiigmgWLDRLDLIAWIQLILDEQPDASIILHGGSMGASTIMMASGEKLPSAV--KGF 199
Cdd:pfam12697  16 ALLAAGVAVLAPDLPGHGSSSPP-----PLDLADLADLAALLDELGAARPVVLVGHSLGGAVALAAAAAALVVGVlvAPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488221597  200 ILDSGYVSVYAEF---------RYMLSKITVFPKKMIMRYANHYAQKYAGYSLKQASATRQLGSNH-----LPLLVIHGE 265
Cdd:pfam12697  91 AAPPGLLAALLALlarlgaalaAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALLPLAawrdlPVPVLVLAE 170
                         170       180       190
                  ....*....|....*....|....*....|..
gi 488221597  266 RDHFVPTEAAYTIqnATAGDKALLLVPEAEHL 297
Cdd:pfam12697 171 EDRLVPELAQRLL--AALAGARLVVLPGAGHL 200
 
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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