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Conserved domains on  [gi|13937355|ref|NP_058599|]
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S-formylglutathione hydrolase isoform 2 [Mus musculus]

Protein Classification

S-formylglutathione hydrolase( domain architecture ID 10010793)

S-formylglutathione hydrolase (FGH) is a serine hydrolase involved in the detoxification of formaldehyde

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
2-281 6.71e-163

S-formylglutathione hydrolase


:

Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 453.46  E-value: 6.71e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    2 ALKQISSNRCFGGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   82 DTSPRGCNIKGEDDSWDFGTGAGFYVNATEDPWKaNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  161 KNPGKYRSVSAFAPICNPVLCSWGKKAFSGYLGPDESKWKAYDATCLVKAYSGSQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 13937355  241 AACTEKKIPVVFRLQEGYDHSYYFIATFIADHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
2-281 6.71e-163

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 453.46  E-value: 6.71e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    2 ALKQISSNRCFGGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   82 DTSPRGCNIKGEDDSWDFGTGAGFYVNATEDPWKaNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  161 KNPGKYRSVSAFAPICNPVLCSWGKKAFSGYLGPDESKWKAYDATCLVKAYSGSQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 13937355  241 AACTEKKIPVVFRLQEGYDHSYYFIATFIADHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
6-280 5.24e-160

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: 445.76  E-value: 5.24e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355     6 ISSNRCFGGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    86 RGCNIKGEDDSWDFGTGAGFYVNATEDPWKANYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   166 YRSVSAFAPICNPVLCSWGKKAFSGYLGPDESKWKAYDATCLVKAySGSQIDILIDQGKDDEFLSNgQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVAD-GGRHSTILIDQGTADQFLDE-QLRPDAFEQACRA 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13937355   246 KKIPVVFRLQEGYDHSYYFIATFIADHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-281 2.07e-112

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 324.09  E-value: 2.07e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  13 GGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627   1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  93 eddswdfGTGAGFYVNATEDPWKaNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYRSVS 170
Cdd:COG0627  71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 171 AFAPICNPVLCSWGKKAFSGYLG-PDESKWKAYDATCLVKAYsGSQIDILIDQGKDDEFLSNGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKL-RAGLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218
                       250       260       270
                ....*....|....*....|....*....|..
gi 13937355 250 VVFRLQEGYdHSYYFIATFIADHIRHHAKYLN 281
Cdd:COG0627 219 HTYRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
23-275 2.21e-78

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: 237.74  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    23 SVELKCKMRFAVYLP-PQAESGKCPALYWLSGlTCTEQNFISKSGYQQAASEHGLVVIAPDTSPRGCNIKGeDDSWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   102 gagfyVNATEDPWKANYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   182 SWGKkafsgylgPDESKWKAYDATCLVKA--YSGSQIDILIDQGKDDEFLsNGQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAVAlsANNTRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELAeqLAYRGVGG 221
                         250       260
                  ....*....|....*....|....*
gi 13937355   258 YDHSY-------YFIATFIADHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
2-281 6.71e-163

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 453.46  E-value: 6.71e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    2 ALKQISSNRCFGGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   82 DTSPRGCNIKGEDDSWDFGTGAGFYVNATEDPWKaNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  161 KNPGKYRSVSAFAPICNPVLCSWGKKAFSGYLGPDESKWKAYDATCLVKAYSGSQIDILIDQGKDDEFLSNgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 13937355  241 AACTEKKIPVVFRLQEGYDHSYYFIATFIADHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
6-280 5.24e-160

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: 445.76  E-value: 5.24e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355     6 ISSNRCFGGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    86 RGCNIKGEDDSWDFGTGAGFYVNATEDPWKANYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   166 YRSVSAFAPICNPVLCSWGKKAFSGYLGPDESKWKAYDATCLVKAySGSQIDILIDQGKDDEFLSNgQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVAD-GGRHSTILIDQGTADQFLDE-QLRPDAFEQACRA 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 13937355   246 KKIPVVFRLQEGYDHSYYFIATFIADHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-281 2.07e-112

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 324.09  E-value: 2.07e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  13 GGLQKVFEHSSVELKCKMRFAVYLPPQAESGKCPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627   1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  93 eddswdfGTGAGFYVNATEDPWKaNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYRSVS 170
Cdd:COG0627  71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 171 AFAPICNPVLCSWGKKAFSGYLG-PDESKWKAYDATCLVKAYsGSQIDILIDQGKDDEFLSNGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGpPDRAAWAANDPLALAEKL-RAGLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218
                       250       260       270
                ....*....|....*....|....*....|..
gi 13937355 250 VVFRLQEGYdHSYYFIATFIADHIRHHAKYLN 281
Cdd:COG0627 219 HTYRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
23-275 2.21e-78

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: 237.74  E-value: 2.21e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    23 SVELKCKMRFAVYLP-PQAESGKCPALYWLSGlTCTEQNFISKSGYQQAASEHGLVVIAPDTSPRGCNIKGeDDSWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   102 gagfyVNATEDPWKANYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355   182 SWGKkafsgylgPDESKWKAYDATCLVKA--YSGSQIDILIDQGKDDEFLsNGQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAVAlsANNTRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELAeqLAYRGVGG 221
                         250       260
                  ....*....|....*....|....*
gi 13937355   258 YDHSY-------YFIATFIADHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
13-262 5.76e-22

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 92.99  E-value: 5.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  13 GGLQKVFEHSSVeLKCKMRFAVYLPPQAESG--KCPALYWLSGLTCTEQNFISKSGYQQAA----SEHGL---VVIAPDt 83
Cdd:COG2382  79 GTVETVTYPSKA-LGRTRRVWVYLPPGYDNPgkKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPD- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  84 sprgcNIKGEDDSWDFGTGAGFyvnatedpwkanyrmYSYVTEELPQLINANFPV--DPQRMSIFGHSMGGHGALICALK 161
Cdd:COG2382 157 -----GGDGGDRGTEGPGNDAF---------------ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALR 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 162 NPGKYRSVSafapicnpvlcswgkkAFSGYLGPDESKWKAYDATCLVKAYS-GSQIDILIDQGKDDEFLSNGQllpdNFI 240
Cdd:COG2382 217 HPDLFGYVG----------------SFSGSFWWPPGDADRGGWAELLAAGApKKPLRFYLDVGTEDDLLEANR----ALA 276
                       250       260
                ....*....|....*....|..
gi 13937355 241 AACTEKKIPVVFRLQEGyDHSY 262
Cdd:COG2382 277 AALKAKGYDVEYREFPG-GHDW 297
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-274 2.89e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 61.96  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  34 VYLPPqaESGKCPALYWLSGLTCTEQNFISksGYQQAASEHGLVVIAPDtsPRGC----NIKGEDDSWDFGTGAGFyvnA 109
Cdd:COG1506  14 LYLPA--DGKKYPVVVYVHGGPGSRDDSFL--PLAQALASRGYAVLAPD--YRGYgesaGDWGGDEVDDVLAAIDY---L 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 110 TEDPWkanyrmysyvteelpqlinanfpVDPQRMSIFGHSMGGHGALICALKNPGKYRSVSAFAPICNPVLCSWGKKAFS 189
Cdd:COG1506  85 AARPY-----------------------VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYT 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 190 -GYLGPDESKWKAYDATCLVKAYSGSQIDILIDQGKDDEF--LSNGQllpdNFIAACTEKKIPVVFRLQEGYDHSYYF-- 264
Cdd:COG1506 142 eRLMGGPWEDPEAYAARSPLAYADKLKTPLLLIHGEADDRvpPEQAE----RLYEALKKAGKPVELLVYPGEGHGFSGag 217
                       250
                ....*....|....*..
gi 13937355 265 -------IATFIADHIR 274
Cdd:COG1506 218 apdylerILDFLDRHLK 234
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
34-261 1.98e-08

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 53.84  E-value: 1.98e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  34 VYLPP--QAESGKCPALYWLSGltctEQNFISKSGYQQAASEHG-----LVVIA----PDTSPR-----GCNIKGEDDSW 97
Cdd:COG2819  25 VYLPPgyDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGigngDDGERRlrdytPPPAPGYPGPG 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  98 DFGTGAgfyvnatedpwkANYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGkyrsvsAFApicn 177
Cdd:COG2819 101 GPGGGA------------DAFL--RFLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPD------LFG---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 178 pvlcSWGkkAFSGYLGPDESKWKAYDATCLVKAYSGSQIDILI---DQGKDDEFLSNGQLLpDNFIAACTEKKIPVVFRL 254
Cdd:COG2819 157 ----RYI--AISPSLWWDDGALLDEAEALLKRSPLPKRLYLSVgtlEGDSMDGMVDDARRL-AEALKAKGYPGLNVKFEV 229

                ....*..
gi 13937355 255 QEGYDHS 261
Cdd:COG2819 230 FPGETHG 236
COG4099 COG4099
Predicted peptidase [General function prediction only];
30-176 2.05e-08

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 53.82  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  30 MRFAVYLPPQAESG-KCPALYWLSG-------LTCTEQNFISKSGYQQAASEHGLVVIAPDTSprgcnikgEDDSWdfgt 101
Cdd:COG4099  33 LPYRLYLPKGYDPGkKYPLVLFLHGagergtdNEKQLTHGAPKFINPENQAKFPAIVLAPQCP--------EDDYW---- 100
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13937355 102 gagfyvnatedpwkanyrMYSYVTEELPQLIN---ANFPVDPQRMSIFGHSMGGHGALICALKNPGKYrsvSAFAPIC 176
Cdd:COG4099 101 ------------------SDTKALDAVLALLDdliAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPIC 157
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
31-173 1.78e-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: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  31 RFAVYLPPQAESGK-CPALYWLSGLTCTEQNFISKSGYQQAASEHGLVVIAPDTSPRGCNIkgeddSWDFGTGAGFYVNA 109
Cdd:COG3509  38 TYRLYVPAGYDGGApLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGR-----CWNWFDGRDQRRGR 112
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13937355 110 TEdpwkanyrmYSYVTeelpQLIN---ANFPVDPQRMSIFGHSMGGHGALICALKNPGKYRSVSAFA 173
Cdd:COG3509 113 DD---------VAFIA----ALVDdlaARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
73-262 6.24e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.03  E-value: 6.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  73 EHGLVVIAPDTsprgcnikgeddswdFGTGAGfyvnaTEDPWKANYRMYSYVTEELPQLINA-------NFPVDPQRMSI 145
Cdd:COG0412  54 AAGYVVLAPDL---------------YGRGGP-----GDDPDEARALMGALDPELLAADLRAaldwlkaQPEVDAGRVGV 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355 146 FGHSMGGHGALICALKNPGkyrsVSAFApicnpvlcswgkkAFSGYLGPDESKWKAYDATClvkaysgsqiDILIDQGKD 225
Cdd:COG0412 114 VGFCFGGGLALLAAARGPD----LAAAV-------------SFYGGLPADDLLDLAARIKA----------PVLLLYGEK 166
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 13937355 226 DEFLSNGQLlpDNFIAACTEKKIPVVFRLQEGYDHSY 262
Cdd:COG0412 167 DPLVPPEQV--AALEAALAAAGVDVELHVYPGAGHGF 201
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
34-156 1.05e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 39.51  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  34 VYLPPqAESGKCPALYWLSGLTcteQNFISKSGYQQAASEHGLVVIAPDtsPRGcnikgeddswdFGTGAGFYVNAtEDP 113
Cdd:COG1073  27 LYLPA-GASKKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFD--YRG-----------YGESEGEPREE-GSP 88
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13937355 114 WKANYR-MYSYVTEeLPQlinanfpVDPQRMSIFGHSMGGHGAL 156
Cdd:COG1073  89 ERRDARaAVDYLRT-LPG-------VDPERIGLLGISLGGGYAL 124
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
73-196 1.76e-03

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 39.32  E-value: 1.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  73 EHGLVVIAPDtsPRGCNikgEDDSWDFGTGAGFYVNATEdpWKANYRMYSYVTEELpQLINANFP-----VDPQRMSIFG 147
Cdd:COG4188  87 SHGYVVAAPD--HPGSN---AADLSAALDGLADALDPEE--LWERPLDLSFVLDQL-LALNKSDPplagrLDLDRIGVIG 158
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 13937355 148 HSMGGHGALICAlknpGKYRSVSAFAPICNPVL---CSWGKKAFSGYLGPDE 196
Cdd:COG4188 159 HSLGGYTALALA----GARLDFAALRQYCGKNPdlqCRALDLPRLAYDLRDP 206
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
46-169 5.48e-03

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: 37.29  E-value: 5.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355  46 PALYWLSGLTCTEQNFisksGYQQAASEHGLVVIAPDtsPRGcnikgeddswdFGtgagfyvnATEDPWkANYRMYSYVt 125
Cdd:COG0596  24 PPVVLLHGLPGSSYEW----RPLIPALAAGYRVIAPD--LRG-----------HG--------RSDKPA-GGYTLDDLA- 76
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 13937355 126 EELPQLINAnfpVDPQRMSIFGHSMGGHGALICALKNPGKYRSV 169
Cdd:COG0596  77 DDLAALLDA---LGLERVVLVGHSMGGMVALELAARHPERVAGL 117
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
65-175 6.98e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 36.82  E-value: 6.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13937355    65 SGYQQAASEHGLVVIAPDtsPRGCNIKGEDdswdfgtgagFYVNATEDpWKANyrmysyvteELPQLINA------NFPV 138
Cdd:pfam00326   4 SWNAQLLADRGYVVAIAN--GRGSGGYGEA----------FHDAGKGD-LGQN---------EFDDFIAAaeylieQGYT 61
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 13937355   139 DPQRMSIFGHSMGGHGALICALKNPGKYRSVSAFAPI 175
Cdd:pfam00326  62 DPDRLAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPV 98
 
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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