NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1440106085|emb|STQ54260|]
View 

putative esterase [Escherichia coli]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
8-276 7.43e-135

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member PLN02442:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 283  Bit Score: 382.20  E-value: 7.43e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085   8 RCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDTSPRGEQ 87
Cdd:PLN02442   12 KMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPRGLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  88 V-ANDDGYDLGQGAGFYLNATQPPWaTHYRMYDYLRDELPALIQSQFNVSD--RCAISGHSMGGHGALIMALKNPGKYTS 164
Cdd:PLN02442   92 VeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQLDtsRASIFGHSMGGHGALTIYLKNPDKYKS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 165 VSAFAPIVNPCSVPWGIKAFSTYLGEDKNAWLEWDSCALMYASNAQDAiPTLIDQGDNDQFLADQLQPAVLAEAARQKAW 244
Cdd:PLN02442  171 VSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSA-TILIDQGEADKFLKEQLLPENFEEACKEAGA 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1440106085 245 PMTLRIQPRYDHSYYFIASFIEDHLRFHAQHL 276
Cdd:PLN02442  250 PVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
8-276 7.43e-135

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 382.20  E-value: 7.43e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085   8 RCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDTSPRGEQ 87
Cdd:PLN02442   12 KMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPRGLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  88 V-ANDDGYDLGQGAGFYLNATQPPWaTHYRMYDYLRDELPALIQSQFNVSD--RCAISGHSMGGHGALIMALKNPGKYTS 164
Cdd:PLN02442   92 VeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQLDtsRASIFGHSMGGHGALTIYLKNPDKYKS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 165 VSAFAPIVNPCSVPWGIKAFSTYLGEDKNAWLEWDSCALMYASNAQDAiPTLIDQGDNDQFLADQLQPAVLAEAARQKAW 244
Cdd:PLN02442  171 VSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSA-TILIDQGEADKFLKEQLLPENFEEACKEAGA 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1440106085 245 PMTLRIQPRYDHSYYFIASFIEDHLRFHAQHL 276
Cdd:PLN02442  250 PVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
2-276 9.56e-129

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 366.41  E-value: 9.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085   2 EMLEEHRCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  82 SPRGEQVAN-DDGYDLGQGAGFYLNATQPPWATHYRMYDYLRDELPALIQSQFNVS-DRCAISGHSMGGHGALIMALKNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDgERQGITGHSMGGHGALVIALKNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 160 GKYTSVSAFAPIVNPCSVPWGIKAFSTYLGEDKNAWLEWDSCALMYASNAQDAIptLIDQGDNDQFLADQLQPAVLAEAA 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTI--LIDQGTADQFLDEQLRPDAFEQAC 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1440106085 240 RQKAWPMTLRIQPRYDHSYYFIASFIEDHLRFHAQHL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-276 1.90e-99

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 291.35  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  12 GWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDtsprgeqvand 91
Cdd:COG0627     2 GRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  92 dgydlGQGAGFYLNATQPPwATHYRMYDYLRDELPALIQSQFNVS---DRCAISGHSMGGHGALIMALKNPGKYTSVSAF 168
Cdd:COG0627    71 -----GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSadrERRAIAGLSMGGHGALTLALRHPDLFRAVAAF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 169 APIVNPCSVPWGIKAFSTYLG-EDKNAWLEWDSCALMyaSNAQDAIPTLIDQGDNDQ-FLADQLQpavLAEAARQKAWPM 246
Cdd:COG0627   145 SGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALA--EKLRAGLPLYIDCGTADPfFLEANRQ---LHAALRAAGIPH 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 1440106085 247 TLRIQPRYdHSYYFIASFIEDHLRFHAQHL 276
Cdd:COG0627   220 TYRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
21-271 4.38e-73

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 224.26  E-value: 4.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  21 SSTLNCPMTFSIFLPPPRDHTPPP-VLYWLSGlTCNDDNFTTKAGAQRVAAELGIVLVMPDTSPRGEQVANDDGYDLGqg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGRKYpVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 100 agfyLNATQPPWATHYRmyDYLRDELPALIQSQFNVSDR-CAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDgRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 179 WGIkafstylgEDKNAWLEWDSCALMYA-SNAQDAIPTLIDQGDNDQFLADQLQPAVLAEAARQKAWP--MTLRIQPRYD 255
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLAVAlSANNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGGYD 223
                         250       260
                  ....*....|....*....|...
gi 1440106085 256 HSY-------YFIASFIEDHLRF 271
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
8-276 7.43e-135

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 382.20  E-value: 7.43e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085   8 RCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDTSPRGEQ 87
Cdd:PLN02442   12 KMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPDTSPRGLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  88 V-ANDDGYDLGQGAGFYLNATQPPWaTHYRMYDYLRDELPALIQSQFNVSD--RCAISGHSMGGHGALIMALKNPGKYTS 164
Cdd:PLN02442   92 VeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQLDtsRASIFGHSMGGHGALTIYLKNPDKYKS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 165 VSAFAPIVNPCSVPWGIKAFSTYLGEDKNAWLEWDSCALMYASNAQDAiPTLIDQGDNDQFLADQLQPAVLAEAARQKAW 244
Cdd:PLN02442  171 VSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSA-TILIDQGEADKFLKEQLLPENFEEACKEAGA 249
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1440106085 245 PMTLRIQPRYDHSYYFIASFIEDHLRFHAQHL 276
Cdd:PLN02442  250 PVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
2-276 9.56e-129

S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and human, with a conserved critical role in formaldehyde detoxification as S-formylglutathione hydrolase (EC 3.1.2.12). Members in eukaryotes such as the human protein are better known as esterase D (EC 3.1.1.1), an enzyme with broad specificity, although S-formylglutathione hydrolase has now been demonstrated as well. [Cellular processes, Detoxification]


Pssm-ID: 131868  Cd Length: 275  Bit Score: 366.41  E-value: 9.56e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085   2 EMLEEHRCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  82 SPRGEQVAN-DDGYDLGQGAGFYLNATQPPWATHYRMYDYLRDELPALIQSQFNVS-DRCAISGHSMGGHGALIMALKNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDgERQGITGHSMGGHGALVIALKNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 160 GKYTSVSAFAPIVNPCSVPWGIKAFSTYLGEDKNAWLEWDSCALMYASNAQDAIptLIDQGDNDQFLADQLQPAVLAEAA 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTI--LIDQGTADQFLDEQLRPDAFEQAC 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1440106085 240 RQKAWPMTLRIQPRYDHSYYFIASFIEDHLRFHAQHL 276
Cdd:TIGR02821 239 RAAGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
12-276 1.90e-99

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 291.35  E-value: 1.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  12 GWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDDNFTTKAGAQRVAAELGIVLVMPDtsprgeqvand 91
Cdd:COG0627     2 GRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  92 dgydlGQGAGFYLNATQPPwATHYRMYDYLRDELPALIQSQFNVS---DRCAISGHSMGGHGALIMALKNPGKYTSVSAF 168
Cdd:COG0627    71 -----GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSadrERRAIAGLSMGGHGALTLALRHPDLFRAVAAF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 169 APIVNPCSVPWGIKAFSTYLG-EDKNAWLEWDSCALMyaSNAQDAIPTLIDQGDNDQ-FLADQLQpavLAEAARQKAWPM 246
Cdd:COG0627   145 SGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALA--EKLRAGLPLYIDCGTADPfFLEANRQ---LHAALRAAGIPH 219
                         250       260       270
                  ....*....|....*....|....*....|
gi 1440106085 247 TLRIQPRYdHSYYFIASFIEDHLRFHAQHL 276
Cdd:COG0627   220 TYRERPGG-HSWYYWASFLEDHLPFLARAL 248
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
21-271 4.38e-73

Putative esterase; This family contains Esterase D. However it is not clear if all members of the family have the same function. This family is related to the pfam00135 family.


Pssm-ID: 395613 [Multi-domain]  Cd Length: 246  Bit Score: 224.26  E-value: 4.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  21 SSTLNCPMTFSIFLPPPRDHTPPP-VLYWLSGlTCNDDNFTTKAGAQRVAAELGIVLVMPDTSPRGEQVANDDGYDLGqg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYPPGRKYpVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 100 agfyLNATQPPWATHYRmyDYLRDELPALIQSQFNVSDR-CAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDgRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 179 WGIkafstylgEDKNAWLEWDSCALMYA-SNAQDAIPTLIDQGDNDQFLADQLQPAVLAEAARQKAWP--MTLRIQPRYD 255
Cdd:pfam00756 152 WGP--------EDDPAWQEGDPVLLAVAlSANNTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGGYD 223
                         250       260
                  ....*....|....*....|...
gi 1440106085 256 HSY-------YFIASFIEDHLRF 271
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
70-270 4.61e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 49.63  E-value: 4.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  70 AELGIVLVMPDtsPRGEqvanddgydlGQGAGFYLNAtqppwathyrMYDYLRDELPALIQSQFNVSDRCAISGHSMGGH 149
Cdd:COG1506    48 ASRGYAVLAPD--YRGY----------GESAGDWGGD----------EVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085 150 GALIMALKNPGKYTSVSAFAPIVNPCSVPWGIKAFSTYLGED--KNAWLEWDSCALMYASNAQdaIPTLIDQGDND-QFL 226
Cdd:COG1506   106 MALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGpwEDPEAYAARSPLAYADKLK--TPLLLIHGEADdRVP 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1440106085 227 ADQLQpaVLAEAARQKAWPMTLRIQPRYDHSYYF---------IASFIEDHLR 270
Cdd:COG1506   184 PEQAE--RLYEALKKAGKPVELLVYPGEGHGFSGagapdylerILDFLDRHLK 234
COG4099 COG4099
Predicted peptidase [General function prediction only];
74-179 3.16e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 41.11  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  74 IVLVMPDTSPRGeqvaNDDGYDLGQGAGFYLNAT------------QPPWATHYRMYDYLRDELPAL--IQSQFNV-SDR 138
Cdd:COG4099    51 LVLFLHGAGERG----TDNEKQLTHGAPKFINPEnqakfpaivlapQCPEDDYWSDTKALDAVLALLddLIAEYRIdPDR 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1440106085 139 CAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVPW 179
Cdd:COG4099   127 IYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDPANAAN 167
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
116-170 3.02e-03

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 38.43  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1440106085 116 RMYDYLRDELPALIQSQFNVS-DRCAISGHSMGGHGALIMALKNPGKYTSVSAFAP 170
Cdd:COG2819   108 AFLRFLEEELKPYIDKRYRTDpERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
65-160 3.22e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 38.02  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1440106085  65 AQRVAAElGIVLVMPDTSPRGEQVANDDgydlgqgAGFYLNATQPPWATHYRMYDYLRdelpALIQSQFNVSDRCAISGH 144
Cdd:COG0412    49 ARRLAAA-GYVVLAPDLYGRGGPGDDPD-------EARALMGALDPELLAADLRAALD----WLKAQPEVDAGRVGVVGF 116
                          90
                  ....*....|....*.
gi 1440106085 145 SMGGHGALIMALKNPG 160
Cdd:COG0412   117 CFGGGLALLAAARGPD 132
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH