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Conserved domains on  [gi|966936764|ref|XP_014990926|]
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valacyclovir hydrolase isoform X1 [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

 Zoom to residue level

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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, ...
 40-291 5.67e-47

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: 156.70  E-value: 5.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  40 TSAKVAVNGVQLHYQQTGEGGHAVLLLPGMLGSGETdFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAK 119
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYE-WRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 120 DAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGY 199
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALART 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 200 DYfartcekwvdgirqfkhlpdgnicRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFA 279
Cdd:COG0596  152 DL------------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|..
gi 966936764 280 NEFNRLAEGFLQ 291
Cdd:COG0596  208 EAFAAALRDFLA 219
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 40-291 5.67e-47

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: 156.70  E-value: 5.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  40 TSAKVAVNGVQLHYQQTGEGGHAVLLLPGMLGSGETdFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAK 119
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYE-WRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 120 DAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGY 199
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALART 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 200 DYfartcekwvdgirqfkhlpdgnicRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFA 279
Cdd:COG0596  152 DL------------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|..
gi 966936764 280 NEFNRLAEGFLQ 291
Cdd:COG0596  208 EAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 62-276 1.15e-24

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: 99.12  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764   62 AVLLLPGMLGSGEtDFGPQLKNLNKKLFTVVAWDPRGYGHSRPP--DRDFPADFFerdAKDAVDLMKALKFKKVSLLGWS 139
Cdd:pfam00561   2 PVLLLHGLPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSSRPkaQDDYRTDDL---AEDLEYILEALGLEKVNLVGHS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  140 DGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTR--------KPLEALYGYDYFARTCEK--- 208
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplGRLVAKLLALLLLRLRLLkal 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  209 -------WVDGIRQFKHLPDGNI----------CRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGK 271
Cdd:pfam00561 158 pllnkrfPSGDYALAKSLVTGALlfietwstelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*
gi 966936764  272 HNLHL 276
Cdd:pfam00561 238 HFAFL 242
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 23-291 2.21e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.48  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  23 GIHVPRAGPAAAFGTsvtsakvaVNGVQLHYQQTGEG-GHAVLLLPGmlgsgetdFGPQLKNLnkkLF---------TVV 92
Cdd:PRK14875 101 GIDEEDAGPAPRKAR--------IGGRTVRYLRLGEGdGTPVVLIHG--------FGGDLNNW---LFnhaalaagrPVI 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  93 AWDPRGYGHSRPPDRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPS------------------ 154
Cdd:PRK14875 162 ALDLPGHGASSKAVGAGSLDEL---AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQrvasltliapaglgpein 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 155 --YIHKMViwGANAYvtdedsmiyegiRDVSKW--------SERTRKPLEALYGYdyfartceKWVDGIRQF-----KHL 219
Cdd:PRK14875 239 gdYIDGFV--AAESR------------RELKPVlellfadpALVTRQMVEDLLKY--------KRLDGVDDAlralaDAL 296

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966936764 220 -PDGNICRHLLPQVQ---CPTLIVHGEKDPLVPRFHANFIHEHVkgsRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 291
Cdd:PRK14875 297 fAGGRQRVDLRDRLAslaIPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 40-291 5.67e-47

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: 156.70  E-value: 5.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  40 TSAKVAVNGVQLHYQQTGEGGHAVLLLPGMLGSGETdFGPQLKNLNKKlFTVVAWDPRGYGHSRPPDRDFPadfFERDAK 119
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGPDGPPVVLLHGLPGSSYE-WRPLIPALAAG-YRVIAPDLRGHGRSDKPAGGYT---LDDLAD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 120 DAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIwganayVTDEDSMIYEGIRDVSKWSERTRKPLEALYGY 199
Cdd:COG0596   78 DLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVL------VDEVLAALAEPLRRPGLAPEALAALLRALART 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 200 DYfartcekwvdgirqfkhlpdgnicRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGKHNLHLRFA 279
Cdd:COG0596  152 DL------------------------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQP 207

                        250
                 ....*....|..
gi 966936764 280 NEFNRLAEGFLQ 291
Cdd:COG0596  208 EAFAAALRDFLA 219
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
59-276 6.59e-25

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 100.02  E-value: 6.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  59 GGHAVLLLPGmLGSGETDFGPQLKNLNKKLFTVVAwdPRGYGHSRPPDrDF----PADFFErDAKDAVDLMKAlKFKKVS 134
Cdd:COG1647   14 GRKGVLLLHG-FTGSPAEMRPLAEALAKAGYTVYA--PRLPGHGTSPE-DLlkttWEDWLE-DVEEAYEILKA-GYDKVI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 135 LLGWSDGGITALIAAAKYPSyIHKMVIWGANAYVTDEDS----MIYEGIRDVSKWSERTRKPLEALYGYDYFartcekWV 210
Cdd:COG1647   88 VIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDPSApllpLLKYLARSLRGIGSDIEDPEVAEYAYDRT------PL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966936764 211 DGIRQFKHLpdGNICRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGS--RLHLMPEGKHNLHL 276
Cdd:COG1647  161 RALAELQRL--IREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPdkELVWLEDSGHVITL 226
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 62-276 1.15e-24

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: 99.12  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764   62 AVLLLPGMLGSGEtDFGPQLKNLNKKLFTVVAWDPRGYGHSRPP--DRDFPADFFerdAKDAVDLMKALKFKKVSLLGWS 139
Cdd:pfam00561   2 PVLLLHGLPGSSD-LWRKLAPALARDGFRVIALDLRGFGKSSRPkaQDDYRTDDL---AEDLEYILEALGLEKVNLVGHS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  140 DGGITALIAAAKYPSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTR--------KPLEALYGYDYFARTCEK--- 208
Cdd:pfam00561  78 MGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVadfapnplGRLVAKLLALLLLRLRLLkal 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  209 -------WVDGIRQFKHLPDGNI----------CRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRLHLMPEGK 271
Cdd:pfam00561 158 pllnkrfPSGDYALAKSLVTGALlfietwstelRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAG 237


                  ....*
gi 966936764  272 HNLHL 276
Cdd:pfam00561 238 HFAFL 242
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
45-284 4.92e-21

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 88.91  E-value: 4.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  45 AVNGVQLHYQQ---TGEGGHAVLLLPGMLGSGETdFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFP-ADFFERDAKD 120
Cdd:COG2267   10 TRDGLRLRGRRwrpAGSPRGTVVLVHGLGEHSGR-YAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDsFDDYVDDLRA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 121 AVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGAnAYVTDEDSMIYEGirdvskwsertrkplealygyd 200
Cdd:COG2267   89 ALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAP-AYRADPLLGPSAR---------------------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 201 yfartcekWVDGIRQFKHlpdgnicrhlLPQVQCPTLIVHGEKDPLVPRFHANFIHEHV-KGSRLHLMPEGKHNLHlrfa 279
Cdd:COG2267  146 --------WLRALRLAEA----------LARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELL---- 203


                 ....*
gi 966936764 280 NEFNR 284
Cdd:COG2267  204 NEPAR 208
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
62-290 5.67e-18

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 80.83  E-value: 5.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  62 AVLLLPGMLGSGETDFGPQLKNLNKKLFTVVAWDPRGYGHSRppdRDFPADFFErDAKDAVDLMKALKF---KKVSLLGW 138
Cdd:COG1506   25 VVVYVHGGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESA---GDWGGDEVD-DVLAAIDYLAARPYvdpDRIGIYGH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 139 SDGGITALIAAAKYPSYIHKMVIWGAnayVTDEDSMiYEGIRDVSKWSERTrkPLEALYGYDyfARTCEKWVDGIRqfkh 218
Cdd:COG1506  101 SYGGYMALLAAARHPDRFKAAVALAG---VSDLRSY-YGTTREYTERLMGG--PWEDPEAYA--ARSPLAYADKLK---- 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966936764 219 lpdgnicrhllpqvqCPTLIVHGEKDPLVP-----RFHANFIhEHVKGSRLHLMPEGKHNLHLRFANEFNRLAEGFL 290
Cdd:COG1506  169 ---------------TPLLLIHGEADDRVPpeqaeRLYEALK-KAGKPVELLVYPGEGHGFSGAGAPDYLERILDFL 229
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 89-273 3.12e-13

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 68.02  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  89 FTVVAWDPRGYGHS--RPPDRDFPAdffERDAKDAVDLMKALKF---KKVSLLGWSDGGITALIAAAKYPsyihkmviwG 163
Cdd:COG1073   65 FNVLAFDYRGYGESegEPREEGSPE---RRDARAAVDYLRTLPGvdpERIGLLGISLGGGYALNAAATDP---------R 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 164 ANAYVTDedSMIYEgIRDVSKwsERTRKPLEALYGYDYFaRTCEKWVDGIR-QFKHLpdgnicrHLLPQVQCPTLIVHGE 242
Cdd:COG1073  133 VKAVILD--SPFTS-LEDLAA--QRAKEARGAYLPGVPY-LPNVRLASLLNdEFDPL-------AKIEKISRPLLFIHGE 199

                        170       180       190
                 ....*....|....*....|....*....|..
gi 966936764 243 KDPLVPRFHANFIHEHVKGS-RLHLMPEGKHN 273
Cdd:COG1073  200 KDEAVPFYMSEDLYEAAAEPkELLIVPGAGHV 231
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 63-277 3.46e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 58.64  E-value: 3.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764   63 VLLLPGMlgsgeTDFGPQLKNLNKKLFTVVAWDPRGYGHSRPPDRDFPadfferDAKDAVDLMKALK-FKKVSLLGWSDG 141
Cdd:pfam12697   1 VVLVHGA-----GLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLA------DLADLAALLDELGaARPVVLVGHSLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  142 GITALIAAAkypSYIHKMVIWGANAYVTDEDSMIYEGIRDVSKWSERTRKPLEALYGYDYFARTC--EKWVDGIRQFKHL 219
Cdd:pfam12697  70 GAVALAAAA---AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPadAEWAAALARLAAL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  220 PDGN--ICRHLLPQVQCPTLIVHGEkDPLVPRFHANFIHEhVKGSRLHLMPEGKHNLHLR 277
Cdd:pfam12697 147 LAALalLPLAAWRDLPVPVLVLAEE-DRLVPELAQRLLAA-LAGARLVVLPGAGHLPLDD 204
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 62-275 2.80e-09

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: 56.45  E-value: 2.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764   62 AVLLLPGMlgsGET-----DFGpqlKNLNKKLFTVVAWDPRGYGHSRPPDRDFPA-DFFERDAKDAVDLMKAL-KFKKVS 134
Cdd:pfam12146   6 VVVLVHGL---GEHsgryaHLA---DALAAQGFAVYAYDHRGHGRSDGKRGHVPSfDDYVDDLDTFVDKIREEhPGLPLF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  135 LLGWSDGGITALIAAAKYPSYIHKMVIWGAnAYVTDEDSM-----------------IYEGIRDVSKWSERTRKPLEAlY 197
Cdd:pfam12146  80 LLGHSMGGLIAALYALRYPDKVDGLILSAP-ALKIKPYLAppilkllakllgklfprLRVPNNLLPDSLSRDPEVVAA-Y 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  198 GYDyfartceKWVDG---IRQFKHLPD-GNICRHLLPQVQCPTLIVHGEKDPLVP-----RFHANFIHEHVkgsRLHLMP 268
Cdd:pfam12146 158 AAD-------PLVHGgisARTLYELLDaGERLLRRAAAITVPLLLLHGGADRVVDpagsrEFYERAGSTDK---TLKLYP 227


                  ....*..
gi 966936764  269 EGKHNLH 275
Cdd:pfam12146 228 GLYHELL 234
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 23-291 2.21e-07

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 51.48  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  23 GIHVPRAGPAAAFGTsvtsakvaVNGVQLHYQQTGEG-GHAVLLLPGmlgsgetdFGPQLKNLnkkLF---------TVV 92
Cdd:PRK14875 101 GIDEEDAGPAPRKAR--------IGGRTVRYLRLGEGdGTPVVLIHG--------FGGDLNNW---LFnhaalaagrPVI 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  93 AWDPRGYGHSRPPDRDFPADFFerdAKDAVDLMKALKFKKVSLLGWSDGGITALIAAAKYPS------------------ 154
Cdd:PRK14875 162 ALDLPGHGASSKAVGAGSLDEL---AAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQrvasltliapaglgpein 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 155 --YIHKMViwGANAYvtdedsmiyegiRDVSKW--------SERTRKPLEALYGYdyfartceKWVDGIRQF-----KHL 219
Cdd:PRK14875 239 gdYIDGFV--AAESR------------RELKPVlellfadpALVTRQMVEDLLKY--------KRLDGVDDAlralaDAL 296

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966936764 220 -PDGNICRHLLPQVQ---CPTLIVHGEKDPLVPRFHANFIHEHVkgsRLHLMPEGKHNLHLRFANEFNRLAEGFLQ 291
Cdd:PRK14875 297 fAGGRQRVDLRDRLAslaIPVLVIWGEQDRIIPAAHAQGLPDGV---AVHVLPGAGHMPQMEAAADVNRLLAEFLG 369
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
62-286 1.26e-04

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 42.26  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  62 AVLLLPGMLGSGET--DFGPQLKNLNkklFTVVAWDPRGYGHSRPPDRD-------FPADFFERDAKDAVDLMKALKF-- 130
Cdd:COG0412   31 GVVVLHEIFGLNPHirDVARRLAAAG---YVVLAPDLYGRGGPGDDPDEaralmgaLDPELLAADLRAALDWLKAQPEvd 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 131 -KKVSLLGWSDGGITALIAAAKYPsyihkmviwGANAYVtdedsmiyegirdvskwsertrkpleALYGydyfartcekw 209
Cdd:COG0412  108 aGRVGVVGFCFGGGLALLAAARGP---------DLAAAV--------------------------SFYG----------- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 210 vdgirqfkhLPDGNICRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGS----RLHLMPEGKHNLHLRFANEFNRL 285
Cdd:COG0412  142 ---------GLPADDLLDLAARIKAPVLLLYGEKDPLVPPEQVAALEAALAAAgvdvELHVYPGAGHGFTNPGRPRYDPA 212


                 .
gi 966936764 286 A 286
Cdd:COG0412  213 A 213
YpfH COG0400
Predicted esterase [General function prediction only];
56-164 1.89e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  56 TGEGGHAVLLLPGmLGSGETDFGPQLKNLNKKLFTVVAwdPRG-----YGHSRPPDRDFPADFF-ERDAKDAVDLMKA-- 127
Cdd:COG0400    1 GGPAAPLVVLLHG-YGGDEEDLLPLAPELALPGAAVLA--PRApvpegPGGRAWFDLSFLEGREdEEGLAAAAEALAAfi 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966936764 128 --------LKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIWGA 164
Cdd:COG0400   78 delearygIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSG 122
PLN02578 PLN02578
hydrolase
 30-264 2.84e-03

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 38.67  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  30 GPAAAFGTSVTSAKVAVNGVQ---------------------LHYQQTGEGGHAVLLLpgmlGSGETDFG-----PQLKn 83
Cdd:PLN02578  36 GGIVASGVSVMGSSSASQSVQglerlpfkkegynfwtwrghkIHYVVQGEGLPIVLIH----GFGASAFHwryniPELA- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764  84 lnkKLFTVVAWDPRGYGHSRPPDRDFPADFFERDAkdaVDLMKALKFKKVSLLGWSDGGITALIAAAKYPSYIHKMVIW- 162
Cdd:PLN02578 111 ---KKYKVYALDLLGFGWSDKALIEYDAMVWRDQV---ADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVALLn 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936764 163 -----------GANAYVTDEDSM---IYEGIRDVSK--------WSERTRKPLEALYGYDYFARTC--EKWVDGIRQ--- 215
Cdd:PLN02578 185 sagqfgsesreKEEAIVVEETVLtrfVVKPLKEWFQrvvlgflfWQAKQPSRIESVLKSVYKDKSNvdDYLVESITEpaa 264

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966936764 216 --------------FKHLPDGNICRHLLPQVQCPTLIVHGEKDPLVPRFHANFIHEHVKGSRL 264
Cdd:PLN02578 265 dpnagevyyrlmsrFLFNQSRYTLDSLLSKLSCPLLLLWGDLDPWVGPAKAEKIKAFYPDTTL 327
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
 235-248 4.98e-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: 37.54  E-value: 4.98e-03
                          10
                  ....*....|....
gi 966936764  235 PTLIVHGEKDPLVP 248
Cdd:pfam20434 191 PFLIIHGDKDPLVP 204
 
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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