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Conserved domains on  [gi|516736455|ref|WP_018074457|]
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alpha/beta fold hydrolase [Rhizobium ruizarguesonis]

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, ...
2-278 2.22e-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: 157.47  E-value: 2.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   2 STVTTKDGVEIFYKDWGPkTAQPIMFHHGWPLCSDDWDAQMlFFLEKGYRVVAHDRRGHGRSTQVGDGHDMDHYAADAAA 81
Cdd:COG0596    4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  82 VVEHLDLRNTVHVGHSTGGGEATHYVARHGQpqgRVAKLVIIGavppimvkteanpgglpiEVFDGLRKQLADNRAqfyh 161
Cdd:COG0596   82 LLDALGLERVVLVGHSMGGMVALELAARHPE---RVAGLVLVD------------------EVLAALAEPLRRPGL---- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 162 dlpagpfysfnrpgakvlepvinnwwrqgmigGAKAHYDGIKAFSETDFTEDLKIITVPTFVMHGDDDQIVPIADSALLs 241
Cdd:COG0596  137 --------------------------------APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL- 183
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 516736455 242 AKLLQNATLKVYEKFPHGMCTTHADIINPDILAFIKG 278
Cdd:COG0596  184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-278 2.22e-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: 157.47  E-value: 2.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   2 STVTTKDGVEIFYKDWGPkTAQPIMFHHGWPLCSDDWDAQMlFFLEKGYRVVAHDRRGHGRSTQVGDGHDMDHYAADAAA 81
Cdd:COG0596    4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  82 VVEHLDLRNTVHVGHSTGGGEATHYVARHGQpqgRVAKLVIIGavppimvkteanpgglpiEVFDGLRKQLADNRAqfyh 161
Cdd:COG0596   82 LLDALGLERVVLVGHSMGGMVALELAARHPE---RVAGLVLVD------------------EVLAALAEPLRRPGL---- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 162 dlpagpfysfnrpgakvlepvinnwwrqgmigGAKAHYDGIKAFSETDFTEDLKIITVPTFVMHGDDDQIVPIADSALLs 241
Cdd:COG0596  137 --------------------------------APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL- 183
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 516736455 242 AKLLQNATLKVYEKFPHGMCTTHADIINPDILAFIKG 278
Cdd:COG0596  184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
24-258 8.60e-28

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: 107.21  E-value: 8.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   24 PIMFHHGWPLCSDDWDAQMLFFLEKGYRVVAHDRRGHGRSTQVGDGHDM--DHYAADAAAVVEHLDLRNTVHVGHSTGGG 101
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  102 EATHYVARHGQpqgRVAKLVIIGAVPPIMVKTEANPGGLPI--EVFDGLR-KQLADNRAQFYHDLPAGPFYS---FNRPG 175
Cdd:pfam00561  82 IALAYAAKYPD---RVKALVLLGALDPPHELDEADRFILALfpGFFDGFVaDFAPNPLGRLVAKLLALLLLRlrlLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  176 AKVLEPVINNWWRQGMIGGAKAHYdgIKAFSETDFTEDLKIITVPTFVMHGDDDQIVPIaDSALLSAKLLQNATLKVYEK 255
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLF--IETWSTELRAKFLGRLDEPTLIIWGDQDPLVPP-QALEKLAQLFPNARLVVIPD 235

                  ...
gi 516736455  256 FPH 258
Cdd:pfam00561 236 AGH 238
PRK05855 PRK05855
SDR family oxidoreductase;
3-118 2.96e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 69.24  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   3 TVTTKDGVEIFYKDWGPKTAQPIMFHHGWPLCSDDWDaQMLFFLEKGYRVVAHDRRGHGRSTQVGDGHD--MDHYAADAA 80
Cdd:PRK05855   6 TVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWD-GVAPLLADRFRVVAYDVRGAGRSSAPKRTAAytLARLADDFA 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 516736455  81 AVVEHLDLRNTVHV-GHSTGGGEATHYVARHGQPqGRVA 118
Cdd:PRK05855  85 AVIDAVSPDRPVHLlAHDWGSIQGWEAVTRPRAA-GRIA 122
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
2-278 2.22e-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: 157.47  E-value: 2.22e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   2 STVTTKDGVEIFYKDWGPkTAQPIMFHHGWPLCSDDWDAQMlFFLEKGYRVVAHDRRGHGRSTQVGDGHDMDHYAADAAA 81
Cdd:COG0596    4 PRFVTVDGVRLHYREAGP-DGPPVVLLHGLPGSSYEWRPLI-PALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  82 VVEHLDLRNTVHVGHSTGGGEATHYVARHGQpqgRVAKLVIIGavppimvkteanpgglpiEVFDGLRKQLADNRAqfyh 161
Cdd:COG0596   82 LLDALGLERVVLVGHSMGGMVALELAARHPE---RVAGLVLVD------------------EVLAALAEPLRRPGL---- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 162 dlpagpfysfnrpgakvlepvinnwwrqgmigGAKAHYDGIKAFSETDFTEDLKIITVPTFVMHGDDDQIVPIADSALLs 241
Cdd:COG0596  137 --------------------------------APEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPPALARRL- 183
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 516736455 242 AKLLQNATLKVYEKFPHGMCTTHADIINPDILAFIKG 278
Cdd:COG0596  184 AELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
3-277 4.05e-30

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 112.79  E-value: 4.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   3 TVTTKDGVEIFYKDWGPKTAQ--PIMFHHGWPLCSDDWDAQMLFFLEKGYRVVAHDRRGHGRST-QVGDGHDMDHYAADA 79
Cdd:COG2267    7 TLPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDgPRGHVDSFDDYVDDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  80 AAVVEHLDLRNTVHV---GHSTGGGEATHYVARHGQpqgRVAKLVIIGavppimvkteanpgglPIEVFDGLRkqladnr 156
Cdd:COG2267   87 RAALDALRARPGLPVvllGHSMGGLIALLYAARYPD---RVAGLVLLA----------------PAYRADPLL------- 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 157 aqfyhdlpagpfysfnrpgakvlePVINNWWRQGMIggakahydgikafsetdfTEDLKIITVPTFVMHGDDDQIVPIAD 236
Cdd:COG2267  141 ------------------------GPSARWLRALRL------------------AEALARIDVPVLVLHGGADRVVPPEA 178
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 516736455 237 SALLSAKLLQNATLKVYEKFPHGMCT-THADIINPDILAFIK 277
Cdd:COG2267  179 ARRLAARLSPDVELVLLPGARHELLNePAREEVLAAILAWLE 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
24-258 8.60e-28

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: 107.21  E-value: 8.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   24 PIMFHHGWPLCSDDWDAQMLFFLEKGYRVVAHDRRGHGRSTQVGDGHDM--DHYAADAAAVVEHLDLRNTVHVGHSTGGG 101
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFRVIALDLRGFGKSSRPKAQDDYrtDDLAEDLEYILEALGLEKVNLVGHSMGGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  102 EATHYVARHGQpqgRVAKLVIIGAVPPIMVKTEANPGGLPI--EVFDGLR-KQLADNRAQFYHDLPAGPFYS---FNRPG 175
Cdd:pfam00561  82 IALAYAAKYPD---RVKALVLLGALDPPHELDEADRFILALfpGFFDGFVaDFAPNPLGRLVAKLLALLLLRlrlLKALP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  176 AKVLEPVINNWWRQGMIGGAKAHYdgIKAFSETDFTEDLKIITVPTFVMHGDDDQIVPIaDSALLSAKLLQNATLKVYEK 255
Cdd:pfam00561 159 LLNKRFPSGDYALAKSLVTGALLF--IETWSTELRAKFLGRLDEPTLIIWGDQDPLVPP-QALEKLAQLFPNARLVVIPD 235

                  ...
gi 516736455  256 FPH 258
Cdd:pfam00561 236 AGH 238
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
49-260 1.48e-17

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: 79.57  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   49 GYRVVAHDRRGHGRStqvgDGH-----DMDHYAADAAAVVEHLDLRN----TVHVGHSTGGGEATHYVARHgqpQGRVAK 119
Cdd:pfam12146  31 GFAVYAYDHRGHGRS----DGKrghvpSFDDYVDDLDTFVDKIREEHpglpLFLLGHSMGGLIAALYALRY---PDKVDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  120 LVIIGA--------VPPIMVKTEANPG----GLPIEVfDGLRKQLADN---RAQFYHDlpagPFysfnrpgakVLEPVIN 184
Cdd:pfam12146 104 LILSAPalkikpylAPPILKLLAKLLGklfpRLRVPN-NLLPDSLSRDpevVAAYAAD----PL---------VHGGISA 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516736455  185 NWWRQGMIGGAKAhydgikafsetdfTEDLKIITVPTFVMHGDDDQIVPIADSALLSAKL-LQNATLKVYEKFPHGM 260
Cdd:pfam12146 170 RTLYELLDAGERL-------------LRRAAAITVPLLLLHGGADRVVDPAGSREFYERAgSTDKTLKLYPGLYHEL 233
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
3-277 5.49e-16

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 75.05  E-value: 5.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   3 TVTTKDGVEI---FYKdwgPKTAQP---IMFHHGWP-LCSDDWDAQMLFFLEKGYRVVAHDRRGHGRSTQVGDGHDMDhy 75
Cdd:COG1506    1 TFKSADGTTLpgwLYL---PADGKKypvVVYVHGGPgSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVD-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  76 aaDAAAVVEHL------DLRNTVHVGHSTGGGEATHYVARHGQpqgRVAKLVIIGAVPpimvkteanpgglpievfdglr 149
Cdd:COG1506   76 --DVLAAIDYLaarpyvDPDRIGIYGHSYGGYMALLAAARHPD---RFKAAVALAGVS---------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 150 kqladNRAQFYHDLpagpfysfnrpgakvlepvinNWWRQGMIGGAKAHYDGIKAFSETDFTEDLKiitVPTFVMHGDDD 229
Cdd:COG1506  129 -----DLRSYYGTT---------------------REYTERLMGGPWEDPEAYAARSPLAYADKLK---TPLLLIHGEAD 179
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516736455 230 QIVPIADSALLSAKLLQN---ATLKVYEKFPHGMCTTHADIINPDILAFIK 277
Cdd:COG1506  180 DRVPPEQAERLYEALKKAgkpVELLVYPGEGHGFSGAGAPDYLERILDFLD 230
PRK05855 PRK05855
SDR family oxidoreductase;
3-118 2.96e-13

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 69.24  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   3 TVTTKDGVEIFYKDWGPKTAQPIMFHHGWPLCSDDWDaQMLFFLEKGYRVVAHDRRGHGRSTQVGDGHD--MDHYAADAA 80
Cdd:PRK05855   6 TVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWD-GVAPLLADRFRVVAYDVRGAGRSSAPKRTAAytLARLADDFA 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 516736455  81 AVVEHLDLRNTVHV-GHSTGGGEATHYVARHGQPqGRVA 118
Cdd:PRK05855  85 AVIDAVSPDRPVHLlAHDWGSIQGWEAVTRPRAA-GRIA 122
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
29-277 1.32e-12

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 65.73  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  29 HGwpLCSDDWDAQML--FFLEKGYRVVAHDRRGHGRSTQVGDGHDMDHYAADAAAVVEHLDLR-NTVHV-GHSTGGGEAT 104
Cdd:COG1647   22 HG--FTGSPAEMRPLaeALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGyDKVIViGLSMGGLLAL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 105 HYVARHGQpqgrVAKLVIIGavPPIMVKteaNPGGLPIEVFDGLRKQL---------ADNRAQFYHDLPAGPFYSFNRpg 175
Cdd:COG1647  100 LLAARYPD----VAGLVLLS--PALKID---DPSAPLLPLLKYLARSLrgigsdiedPEVAEYAYDRTPLRALAELQR-- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 176 akvlepvinnwwrqgMIGGAKahydgikafsetdftEDLKIITVPTFVMHGDDDQIVPIADSALLSAKL-LQNATLKVYE 254
Cdd:COG1647  169 ---------------LIREVR---------------RDLPKITAPTLIIQSRKDEVVPPESARYIYERLgSPDKELVWLE 218
                        250       260
                 ....*....|....*....|....
gi 516736455 255 KFPHGMCT-THADIINPDILAFIK 277
Cdd:COG1647  219 DSGHVITLdKDREEVAEEILDFLE 242
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
8-258 1.33e-11

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 63.81  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   8 DGVEIFYKDWGPKTAQPIMFHHGWPLCSDDWdaqmLFFLE---KGYRVVAHDRRGHGRSTQVGDGHDMDHYAADAAAVVE 84
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNW----LFNHAalaAGRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLD 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  85 HLDLRNTVHVGHSTGGGEATHYVARHgqPQgRVAKLVIIGavppimvkteanPGGLPIEV----FDGL-----RKQLADN 155
Cdd:PRK14875 193 ALGIERAHLVGHSMGGAVALRLAARA--PQ-RVASLTLIA------------PAGLGPEIngdyIDGFvaaesRRELKPV 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 156 RAQFYHDlpagpfysfnrpGAKVLEPVINNWWRQGMIGGAKahyDGIKAFSET---------DFTEDLKIITVPTFVMHG 226
Cdd:PRK14875 258 LELLFAD------------PALVTRQMVEDLLKYKRLDGVD---DALRALADAlfaggrqrvDLRDRLASLAIPVLVIWG 322
                        250       260       270
                 ....*....|....*....|....*....|..
gi 516736455 227 DDDQIVPIADSALLSAkllqNATLKVYEKFPH 258
Cdd:PRK14875 323 EQDRIIPAAHAQGLPD----GVAVHVLPGAGH 350
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
3-277 9.18e-11

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 60.70  E-value: 9.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   3 TVTTKDGVEIFYKDWGPKTAQP-----IMFHhGWPLCSDDWDAQMLFFLEKGYRVVAHDRRGHGRSTqvGDGHDMDHYAA 77
Cdd:COG1073   14 TFKSRDGIKLAGDLYLPAGASKkypavVVAH-GNGGVKEQRALYAQRLAELGFNVLAFDYRGYGESE--GEPREEGSPER 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  78 -DAAAVVEHLDLRNTVH------VGHSTGGGEATHYVARHgqpqGRVAKLVIIGAvppimvkteanpgglpievFDGLRK 150
Cdd:COG1073   91 rDARAAVDYLRTLPGVDperiglLGISLGGGYALNAAATD----PRVKAVILDSP-------------------FTSLED 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455 151 QLADNRAQFYHD-LPAGPFysfnRPGAKVLEpVINNWWrqgmiggakahydgikafsetDFTEDLKIITVPTFVMHGDDD 229
Cdd:COG1073  148 LAAQRAKEARGAyLPGVPY----LPNVRLAS-LLNDEF---------------------DPLAKIEKISRPLLFIHGEKD 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 516736455 230 QIVPIADSALLSAKLLQNATLKVYEKFPHGMC-TTHADIINPDILAFIK 277
Cdd:COG1073  202 EAVPFYMSEDLYEAAAEPKELLIVPGAGHVDLyDRPEEEYFDKLAEFFK 250
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
25-274 2.03e-09

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 56.33  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   25 IMFHHGWPLCSddwdAQMLFFLEKGYRVVAHDRRGHGRSTqvGDGHDMDHYAADAAAVVEHLDLRNTVHVGHSTGGgeat 104
Cdd:pfam12697   1 VVLVHGAGLSA----APLAALLAAGVAVLAPDLPGHGSSS--PPPLDLADLADLAALLDELGAARPVVLVGHSLGG---- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  105 hYVARHGQPQGRVAKLVIigavppimvkteaNPGGLPIEVFDGLRKQLADNRAqfyhDLPAGPFYSFNRPGAKVLEPVIN 184
Cdd:pfam12697  71 -AVALAAAAAALVVGVLV-------------APLAAPPGLLAALLALLARLGA----ALAAPAWLAAESLARGFLDDLPA 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  185 NW-WRQGMIGGAKAHydgikAFSETDFTEDLKIITVPTFVMHGDDDQIVPIADSALlsaKLLQNATLKVYEKfphgmcTT 263
Cdd:pfam12697 133 DAeWAAALARLAALL-----AALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRLL---AALAGARLVVLPG------AG 198
                         250
                  ....*....|.
gi 516736455  264 HADIINPDILA 274
Cdd:pfam12697 199 HLPLDDPEEVA 209
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
1-149 1.33e-06

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 48.84  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   1 MSTVTTKdGVEIFYKDWGpkTAQPIMFHHGWPLCSDDWDAQMLFFLEKGyRVVAHDRRGHGRSTQVGDGHDMDHYAADAA 80
Cdd:PRK03592   9 MRRVEVL-GSRMAYIETG--EGDPIVFLHGNPTSSYLWRNIIPHLAGLG-RCLAPDLIGMGASDKPDIDYTFADHARYLD 84
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516736455  81 AVVEHLDLRNTVHVGHSTGGGEATHYVARHgqpQGRVAKLVIIGAVPPIMVKTEANPGGlpIEVFDGLR 149
Cdd:PRK03592  85 AWFDALGLDDVVLVGHDWGSALGFDWAARH---PDRVRGIAFMEAIVRPMTWDDFPPAV--RELFQALR 148
YheT COG0429
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
4-130 7.09e-05

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


Pssm-ID: 440198 [Multi-domain]  Cd Length: 323  Bit Score: 43.59  E-value: 7.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455   4 VTTKDGVEIFYkDWGPKTAQP----IMFHhGWPLCSDDWDAQ--MLFFLEKGYRVVAHDRRGHG-------RSTQVGDGh 70
Cdd:COG0429   41 LELPDGDFVDL-DWSDPPAPSkplvVLLH-GLEGSSDSHYARglARALYARGWDVVRLNFRGCGgepnllpRLYHSGDT- 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516736455  71 dmdhyaADAAAVVEHL----DLRNTVHVGHSTGGGEATHYVARHGQPQGRVAKLVIIGavPPIM 130
Cdd:COG0429  118 ------EDLVWVLAHLraryPYAPLYAVGFSLGGNLLLKYLGEQGDDAPPLKAAVAVS--PPLD 173
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
20-125 8.38e-05

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 40.97  E-value: 8.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  20 KTAQPIMFHHGWpLCSD-DWDAQMLFFLEKGYRVVAHDrrghgrstQVGDGHDMDHYAADAAAVVEHLdLRNT----VH- 93
Cdd:COG1075    3 ATRYPVVLVHGL-GGSAaSWAPLAPRLRAAGYPVYALN--------YPSTNGSIEDSAEQLAAFVDAV-LAATgaekVDl 72
                         90       100       110
                 ....*....|....*....|....*....|..
gi 516736455  94 VGHSTGGGEATHYVARHGQPQgRVAKLVIIGA 125
Cdd:COG1075   73 VGHSMGGLVARYYLKRLGGAA-KVARVVTLGT 103
PRK00870 PRK00870
haloalkane dehalogenase; Provisional
14-142 8.97e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 179147 [Multi-domain]  Cd Length: 302  Bit Score: 43.03  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  14 YKDWGPKTAQPIMFHHGWPLCSDDWDAQMLFFLEKGYRVVAHDRRGHGRSTQVGDghDMDH-YAADAA---AVVEHLDLR 89
Cdd:PRK00870  38 YVDEGPADGPPVLLLHGEPSWSYLYRKMIPILAAAGHRVIAPDLIGFGRSDKPTR--REDYtYARHVEwmrSWFEQLDLT 115
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516736455  90 NTVHVGHSTGGGEATHYVARHGQpqgRVAKLVIigavppimvkteANpGGLPI 142
Cdd:PRK00870 116 DVTLVCQDWGGLIGLRLAAEHPD---RFARLVV------------AN-TGLPT 152
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
218-244 1.01e-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: 39.47  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*..
gi 516736455  218 TVPTFVMHGDDDQIVPIADSALLSAKL 244
Cdd:pfam20434 189 DPPFLIIHGDKDPLVPYCQSVLLHEKL 215
YpfH COG0400
Predicted esterase [General function prediction only];
219-277 1.95e-03

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 38.35  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516736455 219 VPTFVMHGDDDQIVPIaDSALLSAKLLQNATLKV-YEKFP--HGMCtthADIINpDILAFIK 277
Cdd:COG0400  140 TPVFLAHGTQDPVIPV-ERAREAAEALEAAGADVtYREYPggHEIS---PEELA-DARAWLA 196
PRK03204 PRK03204
haloalkane dehalogenase; Provisional
12-100 7.90e-03

haloalkane dehalogenase; Provisional


Pssm-ID: 179554 [Multi-domain]  Cd Length: 286  Bit Score: 37.14  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516736455  12 IFYKDWGpkTAQPIMFHHGWPLCSDDWdAQMLFFLEKGYRVVAHDRRGHGRSTQ-VGDGHDMDHYAADAAAVVEHLDLRN 90
Cdd:PRK03204  26 IHYIDEG--TGPPILLCHGNPTWSFLY-RDIIVALRDRFRCVAPDYLGFGLSERpSGFGYQIDEHARVIGEFVDHLGLDR 102
                         90
                 ....*....|
gi 516736455  91 TVHVGHSTGG 100
Cdd:PRK03204 103 YLSMGQDWGG 112
 
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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