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Conserved domains on  [gi|399498543|ref|NP_001257795|]
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S-formylglutathione hydrolase isoform b [Rattus norvegicus]

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

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List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 2-256 2.60e-143

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: 403.00  E-value: 2.60e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   2 ELKQISSNKCFGGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  82 DTSPRGCNIKGEDDSWDFGTGAGFFVNATEDPWNtNYRMYSYVTEELPQLINANFP-VDPQRISIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 161 KNPGKYRSVSAFAPICNPVLCPWGKKAFNGYLGPDQSKWKAYDATCLVKSYSGPQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250
                 ....*....|....*.
gi 399498543 241 AACTEKKIPVVFRLQE 256
Cdd:PLN02442 242 EACKEAGAPVTLRLQP 257
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-256 2.60e-143

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 403.00  E-value: 2.60e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   2 ELKQISSNKCFGGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  82 DTSPRGCNIKGEDDSWDFGTGAGFFVNATEDPWNtNYRMYSYVTEELPQLINANFP-VDPQRISIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 161 KNPGKYRSVSAFAPICNPVLCPWGKKAFNGYLGPDQSKWKAYDATCLVKSYSGPQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250
                 ....*....|....*.
gi 399498543 241 AACTEKKIPVVFRLQE 256
Cdd:PLN02442 242 EACKEAGAPVTLRLQP 257
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 6-256 1.37e-136

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: 385.67  E-value: 1.37e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543    6 ISSNKCFGGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   86 RGCNIKGEDDSWDFGTGAGFFVNATEDPWNTNYRMYSYVTEELPQLINANFPVDPQRISIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  166 YRSVSAFAPICNPVLCPWGKKAFNGYLGPDQSKWKAYDATCLVKSYSGPQiDILIDQGKDDEFLSNgQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHS-TILIDQGTADQFLDE-QLRPDAFEQACRA 240

                         250
                  ....*....|.
gi 399498543  246 KKIPVVFRLQE 256
Cdd:TIGR02821 241 AGQALTLRRQA 251
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-256 3.97e-96

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 282.11  E-value: 3.97e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  13 GGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  93 eddswdfGTGAGFFVNATEDPwNTNYRMYSYVTEELPQLINANFPVDPQR--ISIFGHSMGGHGALICALKNPGKYRSVS 170
Cdd:COG0627   71 -------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 171 AFAPICNPVLCPWGKKAFNGYLG-PDQSKWKAYDATCLVKSYsGPQIDILIDQGKDDEFlsngqLLPDN--FIAACTEKK 247
Cdd:COG0627  143 AFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKL-RAGLPLYIDCGTADPF-----FLEANrqLHAALRAAG 216


                 ....*....
gi 399498543 248 IPVVFRLQE 256
Cdd:COG0627  217 IPHTYRERP 225
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 23-249 6.35e-71

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: 218.10  E-value: 6.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   23 SVELKCKMKFAIYLP-PQAESAKCPALYWLSGlTCTEQNFISKSGCQQAASEHGLVVIAPDTSPRGCNIKGeDDSWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  102 gagffVNATEDPWNTNYRmySYVTEELPQLINANFPVDPQRISIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  182 PWGKkafngylgPDQSKWKAYDATCLVK--SYSGPQIDILIDQGKDDEFLsNGQLLPDNFIAACTEKKIP 249
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELA 211
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-256 2.60e-143

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 403.00  E-value: 2.60e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   2 ELKQISSNKCFGGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  82 DTSPRGCNIKGEDDSWDFGTGAGFFVNATEDPWNtNYRMYSYVTEELPQLINANFP-VDPQRISIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 161 KNPGKYRSVSAFAPICNPVLCPWGKKAFNGYLGPDQSKWKAYDATCLVKSYSGPQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250
                 ....*....|....*.
gi 399498543 241 AACTEKKIPVVFRLQE 256
Cdd:PLN02442 242 EACKEAGAPVTLRLQP 257
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 6-256 1.37e-136

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: 385.67  E-value: 1.37e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543    6 ISSNKCFGGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   86 RGCNIKGEDDSWDFGTGAGFFVNATEDPWNTNYRMYSYVTEELPQLINANFPVDPQRISIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  166 YRSVSAFAPICNPVLCPWGKKAFNGYLGPDQSKWKAYDATCLVKSYSGPQiDILIDQGKDDEFLSNgQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHS-TILIDQGTADQFLDE-QLRPDAFEQACRA 240

                         250
                  ....*....|.
gi 399498543  246 KKIPVVFRLQE 256
Cdd:TIGR02821 241 AGQALTLRRQA 251
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-256 3.97e-96

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 282.11  E-value: 3.97e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  13 GGLQKVFEHSSVELKCKMKFAIYLPPQAESAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  93 eddswdfGTGAGFFVNATEDPwNTNYRMYSYVTEELPQLINANFPVDPQR--ISIFGHSMGGHGALICALKNPGKYRSVS 170
Cdd:COG0627   71 -------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 171 AFAPICNPVLCPWGKKAFNGYLG-PDQSKWKAYDATCLVKSYsGPQIDILIDQGKDDEFlsngqLLPDN--FIAACTEKK 247
Cdd:COG0627  143 AFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKL-RAGLPLYIDCGTADPF-----FLEANrqLHAALRAAG 216


                 ....*....
gi 399498543 248 IPVVFRLQE 256
Cdd:COG0627  217 IPHTYRERP 225
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 23-249 6.35e-71

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: 218.10  E-value: 6.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   23 SVELKCKMKFAIYLP-PQAESAKCPALYWLSGlTCTEQNFISKSGCQQAASEHGLVVIAPDTSPRGCNIKGeDDSWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  102 gagffVNATEDPWNTNYRmySYVTEELPQLINANFPVDPQRISIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  182 PWGKkafngylgPDQSKWKAYDATCLVK--SYSGPQIDILIDQGKDDEFLsNGQLLPDNFIAACTEKKIP 249
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELA 211
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
13-253 7.56e-19

Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 84.13  E-value: 7.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  13 GGLQKVFEHSSVeLKCKMKFAIYLPPQAESA--KCPALYWLSGLTCTEQNFISKSGCQQAA----SEHGL---VVIAPDT 83
Cdd:COG2382   79 GTVETVTYPSKA-LGRTRRVWVYLPPGYDNPgkKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPDG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  84 SPRGcnikgeddswdfgtgagffVNATEDPWNTNYrmYSYVTEELPQLINANFPV--DPQRISIFGHSMGGHGALICALK 161
Cdd:COG2382  158 GDGG-------------------DRGTEGPGNDAF--ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 162 NPGKYRSVSAFApicnpvlcpwgkkafnGYLGPDQSKWKAYDATCLVKSYS-GPQIDILIDQGKDDEFLSNGQllpdNFI 240
Cdd:COG2382  217 HPDLFGYVGSFS----------------GSFWWPPGDADRGGWAELLAAGApKKPLRFYLDVGTEDDLLEANR----ALA 276

                        250
                 ....*....|...
gi 399498543 241 AACTEKKIPVVFR 253
Cdd:COG2382  277 AALKAKGYDVEYR 289
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-252 4.52e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 58.10  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  34 IYLPPQAEsaKCPALYWLSGLTCTEQNFISKSGcqQAASEHGLVVIAPDtsPRGC----NIKGEDDSWDFGTGAGFFVna 109
Cdd:COG1506   14 LYLPADGK--KYPVVVYVHGGPGSRDDSFLPLA--QALASRGYAVLAPD--YRGYgesaGDWGGDEVDDVLAAIDYLA-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543 110 tEDPWntnyrmysyvteelpqlinanfpVDPQRISIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPV----LCPWGK 185
Cdd:COG1506   86 -ARPY-----------------------VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRsyygTTREYT 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 399498543 186 KAFNGYLGPDQSKWKAYDATCLVKSYSGPqidILIDQGKDDEF--LSNGQllpdNFIAACTEKKIPVVF 252
Cdd:COG1506  142 ERLMGGPWEDPEAYAARSPLAYADKLKTP---LLLIHGEADDRvpPEQAE----RLYEALKKAGKPVEL 203
COG4099 COG4099
Predicted peptidase [General function prediction only];
30-176 1.27e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 56.90  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  30 MKFAIYLPPQAESA-KCPALYWLSGltcteqnfISKSGCQ-QAASEHGLVVIApdtsprgcnikgeddSWDFGTGAGFFV 107
Cdd:COG4099   33 LPYRLYLPKGYDPGkKYPLVLFLHG--------AGERGTDnEKQLTHGAPKFI---------------NPENQAKFPAIV 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 399498543 108 ----NATEDPWNTNYRMysyvtEELPQLIN---ANFPVDPQRISIFGHSMGGHGALICALKNPGKYrsvSAFAPIC 176
Cdd:COG4099   90 lapqCPEDDYWSDTKAL-----DAVLALLDdliAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPIC 157
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 32-173 1.57e-07

Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 51.16  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  32 FAIYLPPQAE-SAKCPALYWLSGLTCTEQNFISKSGCQQAASEHGLVVIAPDTSPR-----------GCNIKGEDDswdf 99
Cdd:COG3509   39 YRLYVPAGYDgGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRapgrcwnwfdgRDQRRGRDD---- 114

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399498543 100 gtgAGFFVNATEDpwntnyrmysyvteelpqlINANFPVDPQRISIFGHSMGGHGALICALKNPGKYRSVSAFA 173
Cdd:COG3509  115 ---VAFIAALVDD-------------------LAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
119-174 1.60e-07

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 51.14  E-value: 1.60e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 399498543 119 RMYSYVTEELPQLINANFPVDPQRISIFGHSMGGHGALICALKNPGKYRSVSAFAP 174
Cdd:COG2819  108 AFLRFLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
73-196 4.53e-05

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 43.94  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  73 EHGLVVIAPD-TSPRGCNIKGEDDSWDFGTGAGFFVNATEDpwntnyrMySYVTEELpQLINANFP-----VDPQRISIF 146
Cdd:COG4188   87 SHGYVVAAPDhPGSNAADLSAALDGLADALDPEELWERPLD-------L-SFVLDQL-LALNKSDPplagrLDLDRIGVI 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 399498543 147 GHSMGGHGALICAlknpGKYRSVSAFAPICNPVL---CPWGKKAFNGYLGPDQ 196
Cdd:COG4188  158 GHSLGGYTALALA----GARLDFAALRQYCGKNPdlqCRALDLPRLAYDLRDP 206
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 73-156 2.79e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 38.36  E-value: 2.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  73 EHGLVVIAPDtsPRGcnikgeddswdFGTGAGFFVNAtEDPWNTNYR-MYSYVTEeLPQlinanfpVDPQRISIFGHSMG 151
Cdd:COG1073   62 ELGFNVLAFD--YRG-----------YGESEGEPREE-GSPERRDARaAVDYLRT-LPG-------VDPERIGLLGISLG 119


                 ....*
gi 399498543 152 GHGAL 156
Cdd:COG1073  120 GGYAL 124
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
 74-177 4.99e-03

Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyse the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.


Pssm-ID: 398876 [Multi-domain]  Cd Length: 316  Bit Score: 37.76  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543   74 HGLVVIAPDTspRGCNIKGEDDSWDF--GTGAGFFVNATEDPWNTNYRmysYVTEELPQLIN--ANFP-VDPQRISIFGH 148
Cdd:pfam05448 107 HGYAVFVMDV--RGQGGLSEDDPRGPkgNTYKGHITRGLLDRETYYYR---RVFLDAVRAVEivMSFPeVDEERIVVTGG 181

                          90       100       110
                  ....*....|....*....|....*....|
gi 399498543  149 SMGGHGALICALKNPgKYRSVSAFAP-ICN 177
Cdd:pfam05448 182 SQGGALALAAAALSP-RIKAVVADYPfLSD 210
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
73-174 5.05e-03

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 37.25  E-value: 5.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399498543  73 EHGLVVIAPDTsprgcnikgeddswdFGTGAGffvnaTEDPWNTNYRMYSYVTEELPQLINA-------NFPVDPQRISI 145
Cdd:COG0412   54 AAGYVVLAPDL---------------YGRGGP-----GDDPDEARALMGALDPELLAADLRAaldwlkaQPEVDAGRVGV 113

                         90       100
                 ....*....|....*....|....*....
gi 399498543 146 FGHSMGGHGALICALKNPGkYRSVSAFAP 174
Cdd:COG0412  114 VGFCFGGGLALLAAARGPD-LAAAVSFYG 141
 
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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