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Conserved domains on  [gi|1622936072|ref|XP_028703708|]
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valacyclovir hydrolase isoform X2 [Macaca mulatta]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 38-259 7.08e-38

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: 132.43  E-value: 7.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  38 LGSGETDFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAA 117
Cdd:COG0596    32 LPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLADDLAALLDALGLERVVLVGHSMGGMVALELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 118 AKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYfartcekwvdgirqfkhlpdgnicRHLL 197
Cdd:COG0596   108 ARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL------------------------RERL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936072 198 PQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 259
Cdd:COG0596   158 ARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 38-259 7.08e-38

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: 132.43  E-value: 7.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  38 LGSGETDFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAA 117
Cdd:COG0596    32 LPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLADDLAALLDALGLERVVLVGHSMGGMVALELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 118 AKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYfartcekwvdgirqfkhlpdgnicRHLL 197
Cdd:COG0596   108 ARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL------------------------RERL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936072 198 PQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 259
Cdd:COG0596   158 ARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 37-244 1.12e-21

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: 90.26  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  37 FLGSGEtDFGPQLKNLNKKLFTVVAWDPRGYGHSRPP--DRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITAL 114
Cdd:pfam00561   9 LPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSSRPkaQDDYRTDDL---AEDLEYILEALGLEKVNLVGHSMGGLIAL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 115 IAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTR--------KPLEALYGYDYFARTCEK---------- 176
Cdd:pfam00561  85 AYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplGRLVAKLLALLLLRLRLLkalpllnkrf 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936072 177 WVDGIRQFKHLPDGNI----------CRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHL 244
Cdd:pfam00561 165 PSGDYALAKSLVTGALlfietwstelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-259 2.41e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  58 TVVAWDPRGYGHSRPPDRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPS--------------- 122
Cdd:PRK14875  159 PVIALDLPGHGASSKAVGAGSLDEL---AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQrvasltliapaglgp 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 123 -----YIHKMViwGANAYvtdedsmiyegiRDVSKW--------SERTRKPLEALYGYdyfartceKWVDGIRQF----- 184
Cdd:PRK14875  236 eingdYIDGFV--AAESR------------RELKPVlellfadpALVTRQMVEDLLKY--------KRLDGVDDAlrala 293

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936072 185 KHL-PDGNICRHLLPQVQ---CPTLIVHGEKDPLVPRFHANFIHEHVkgsRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 259
Cdd:PRK14875  294 DALfAGGRQRVDLRDRLAslaIPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 38-259 7.08e-38

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: 132.43  E-value: 7.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  38 LGSGETDFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAA 117
Cdd:COG0596    32 LPGSSYEWRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLADDLAALLDALGLERVVLVGHSMGGMVALELA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 118 AKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYfartcekwvdgirqfkhlpdgnicRHLL 197
Cdd:COG0596   108 ARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALARTDL------------------------RERL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622936072 198 PQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 259
Cdd:COG0596   158 ARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
38-244 1.06e-22

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 93.08  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  38 LGSGETDFGPQLKNLNKKLFTVVAwdPRGYGHSRPPDrDF----PADFFErDAKDAVDLMKAlKFKKVSLLGWSDGGITA 113
Cdd:COG1647    24 FTGSPAEMRPLAEALAKAGYTVYA--PRLPGHGTSPE-DLlkttWEDWLE-DVEEAYEILKA-GYDKVIVIGLSMGGLLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 114 LIAAAKYPSyIHKMVIWGANAYVTDEDS----MIYEGIRDVSKWSERTRKPLEALYGYDYFartcekWVDGIRQFKHLpd 189
Cdd:COG1647    99 LLLAARYPD-VAGLVLLSPALKIDDPSApllpLLKYLARSLRGIGSDIEDPEVAEYAYDRT------PLRALAELQRL-- 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622936072 190 GNICRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGS--RLHLMPEGKHNLHL 244
Cdd:COG1647   170 IREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGHVITL 226
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 37-244 1.12e-21

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: 90.26  E-value: 1.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  37 FLGSGEtDFGPQLKNLNKKLFTVVAWDPRGYGHSRPP--DRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITAL 114
Cdd:pfam00561   9 LPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSSRPkaQDDYRTDDL---AEDLEYILEALGLEKVNLVGHSMGGLIAL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 115 IAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTR--------KPLEALYGYDYFARTCEK---------- 176
Cdd:pfam00561  85 AYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplGRLVAKLLALLLLRLRLLkalpllnkrf 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622936072 177 WVDGIRQFKHLPDGNI----------CRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHL 244
Cdd:pfam00561 165 PSGDYALAKSLVTGALlfietwstelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
57-252 1.23e-18

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 81.59  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  57 FTVVAWDPRGYGHSRPPDRDFP-ADFFERDAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGAnAY 135
Cdd:COG2267    56 YAVLAFDLRGHGRSDGPRGHVDsFDDYVDDLRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP-AY 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 136 VTDEDSMIYEGirdvskwsertrkplealygydyfartcekWVDGIRQFKHlpdgnicrhlLPQVQCPTLIVHGEKDPLV 215
Cdd:COG2267   135 RADPLLGPSAR------------------------------WLRALRLAEA----------LARIDVPVLVLHGGADRVV 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622936072 216 PRFHANFIHEHV-KGSRLHLMPEGKHNLHlrfaNEFNR 252
Cdd:COG2267   175 PPEAARRLAARLsPDVELVLLPGARHELL----NEPAR 208
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
57-258 5.98e-18

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 80.06  E-value: 5.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  57 FTVVAWDPRGYGHSRppdRDFPADFFErDAKDAVDLMKALKF---KKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGAn 133
Cdd:COG1506    52 YAVLAPDYRGYGESA---GDWGGDEVD-DVLAAIDYLAARPYvdpDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAG- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 134 ayVTDEDSMiYEGIRDVSKWSERTrkPLEALYGYDyfARTCEKWVDGIRqfkhlpdgnicrhllpqvqCPTLIVHGEKDP 213
Cdd:COG1506   127 --VSDLRSY-YGTTREYTERLMGG--PWEDPEAYA--ARSPLAYADKLK-------------------TPLLLIHGEADD 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622936072 214 LVP-----RFHANFIhEHVKGSRLHLMPEGKHNLHLRFANEFNRLAEGFL 258
Cdd:COG1506   181 RVPpeqaeRLYEALK-KAGKPVELLVYPGEGHGFSGAGAPDYLERILDFL 229
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 57-241 3.52e-14

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 69.94  E-value: 3.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  57 FTVVAWDPRGYGHS--RPPDRDFPAdffERDAKDAVDLMKALKF---KKVSLLGWSDGGITALIAAAKYPsyihkmviwG 131
Cdd:COG1073    65 FNVLAFDYRGYGESegEPREEGSPE---RRDARAAVDYLRTLPGvdpERIGLLGISLGGGYALNAAATDP---------R 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 132 ANAYVTDedSMIYEgIRDVSKwsERTRKPLEALYGYDYFaRTCEKWVDGIR-QFKHLpdgnicrHLLPQVQCPTLIVHGE 210
Cdd:COG1073   133 VKAVILD--SPFTS-LEDLAA--QRAKEARGAYLPGVPY-LPNVRLASLLNdEFDPL-------AKIEKISRPLLFIHGE 199

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622936072 211 KDPLVPRFHANFIHEHVKGS-RLHLMPEGKHN 241
Cdd:COG1073   200 KDEAVPFYMSEDLYEAAAEPkELLIVPGAGHV 231
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 47-245 9.93e-11

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 59.79  E-value: 9.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  47 PQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPadfferDAKDAVDLMKALK-FKKVSLLGWSDGGITALIAAAkypSYIH 125
Cdd:pfam12697  12 APLAALLAAGVAVLAPDLPGHGSSSPPPLDLA------DLADLAALLDELGaARPVVLVGHSLGGAVALAAAA---AALV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 126 KMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTC--EKWVDGIRQFKHLPDGN--ICRHLLPQVQ 201
Cdd:pfam12697  83 VGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPadAEWAAALARLAALLAALalLPLAAWRDLP 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622936072 202 CPTLIVHGEkDPLVPRFHANFIHEhVKGSRLHLMPEGKHNLHLR 245
Cdd:pfam12697 163 VPVLVLAEE-DRLVPELAQRLLAA-LAGARLVVLPGAGHLPLDD 204
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 52-243 8.29e-10

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: 57.61  E-value: 8.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  52 LNKKLFTVVAWDPRGYGHSRPPDRDFPA-DFFERDAKDAVDLMKAL-KFKKVSLLGWSDGGITALIAAAKYPSYIHKMVI 129
Cdd:pfam12146  27 LAAQGFAVYAYDHRGHGRSDGKRGHVPSfDDYVDDLDTFVDKIREEhPGLPLFLLGHSMGGLIAALYALRYPDKVDGLIL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 130 WGAnAYVTDEDSM-----------------IYEGIRDVSKWSERTRKPLEAlYGYDyfartceKWVDG---IRQFKHLPD 189
Cdd:pfam12146 107 SAP-ALKIKPYLAppilkllakllgklfprLRVPNNLLPDSLSRDPEVVAA-YAAD-------PLVHGgisARTLYELLD 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 190 -GNICRHLLPQVQCPTLIVHGEKDPLVP-----RFHANFIHEHVkgsRLHLMPEGKHNLH 243
Cdd:pfam12146 178 aGERLLRRAAAITVPLLLLHGGADRVVDpagsrEFYERAGSTDK---TLKLYPGLYHELL 234
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 58-259 2.41e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.10  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  58 TVVAWDPRGYGHSRPPDRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPS--------------- 122
Cdd:PRK14875  159 PVIALDLPGHGASSKAVGAGSLDEL---AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQrvasltliapaglgp 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 123 -----YIHKMViwGANAYvtdedsmiyegiRDVSKW--------SERTRKPLEALYGYdyfartceKWVDGIRQF----- 184
Cdd:PRK14875  236 eingdYIDGFV--AAESR------------RELKPVlellfadpALVTRQMVEDLLKY--------KRLDGVDDAlrala 293

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622936072 185 KHL-PDGNICRHLLPQVQ---CPTLIVHGEKDPLVPRFHANFIHEHVkgsRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 259
Cdd:PRK14875  294 DALfAGGRQRVDLRDRLAslaIPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
57-254 1.17e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 45.34  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072  57 FTVVAWDPrgYGHSRPPDRD---------FPADFFERDAKDAVDLMKALKF---KKVSLLGWSDGGITALIAAAKYPsyi 124
Cdd:COG0412    57 YVVLAPDL--YGRGGPGDDPdearalmgaLDPELLAADLRAALDWLKAQPEvdaGRVGVVGFCFGGGLALLAAARGP--- 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622936072 125 hkmviwGANAYVtdedsmiyegirdvskwsertrkpleALYGydyfartcekwvdgirqfkhLPDGNICRHLLPQVQCPT 204
Cdd:COG0412   132 ------DLAAAV--------------------------SFYG--------------------GLPADDLLDLAARIKAPV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622936072 205 LIVHGEKDPLVPRFHANFIHEHVKGS----RLHLMPEGKHNLHLRFANEFNRLA 254
Cdd:COG0412   160 LLLYGEKDPLVPPEQVAALEAALAAAgvdvELHVYPGAGHGFTNPGRPRYDPAA 213
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 203-216 2.65e-03

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 37.93  E-value: 2.65e-03
                          10
                  ....*....|....
gi 1622936072 203 PTLIVHGEKDPLVP 216
Cdd:pfam20434 191 PFLIIHGDKDPLVP 204
COG3571 COG3571
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
197-245 5.06e-03

Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];


Pssm-ID: 442792 [Multi-domain]  Cd Length: 202  Bit Score: 37.17  E-value: 5.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622936072 197 LPQVQCPTLIVHGEKDPLVPR--FHANFIHEHVkgsRLHLMPEGKHNLHLR 245
Cdd:COG3571   128 LADLTVPTLIVQGERDPFGTPeeVAGYPLPPAI---ELVWLPGGDHDLKPR 175
 
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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