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Conserved domains on  [gi|33413400|ref|NP_001975|]
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S-formylglutathione hydrolase [Homo sapiens]

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 2.28e-160

S-formylglutathione hydrolase


:

Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 446.92  E-value: 2.28e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    2 ALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   82 DTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  161 KNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 33413400  241 AACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 2.28e-160

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 446.92  E-value: 2.28e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    2 ALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   82 DTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  161 KNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 33413400  241 AACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLN 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 2.04e-158

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: 441.91  E-value: 2.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400     6 ISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    86 RGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   166 YKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYpGSQLDILIDQGKDDQFlLDGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQF-LDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 33413400   246 KKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-281 2.03e-113

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 326.79  E-value: 2.03e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  13 GGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627   1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  93 edeswdfGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG0627  71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 171 AFAPICNPVLCPWGKKAFSGYLGT-DQSKWKAYDATHLVKSYPGsQLDILIDQGKDDQFLLDGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218

                       250       260       270
                ....*....|....*....|....*....|..
gi 33413400 250 VVFRLQEGYdHSYYFIATFITDHIRHHAKYLN 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 1.83e-82

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: 248.14  E-value: 1.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    23 SVELNCKMKFAVYLP-PKAETGKCPALYWLSGlTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGeDESWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   102 gagfyVDATEDPWKTNYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   182 PWGKkafsgylgTDQSKWKAYDATHLVK--SYPGSQLDILIDQGKDDQFLLDgQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFLGD-QLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 33413400   258 YDHSY-------YFIATFITDHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 2.28e-160

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 446.92  E-value: 2.28e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    2 ALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   82 DTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFP-VDPQRMSIFGHSMGGHGALICAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDqLDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  161 KNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDgQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFLKE-QLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 33413400  241 AACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLN 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 2.04e-158

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: 441.91  E-value: 2.04e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400     6 ISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    86 RGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   166 YKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYpGSQLDILIDQGKDDQFlLDGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQF-LDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 33413400   246 KKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
13-281 2.03e-113

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 326.79  E-value: 2.03e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  13 GGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDtsprgcnikg 92
Cdd:COG0627   1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  93 edeswdfGTGAGFYVDATEDPWKtNYRMYSYVTEELPQLINANFPVDPQR--MSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG0627  71 -------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSADRerRAIAGLSMGGHGALTLALRHPDLFRAVA 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 171 AFAPICNPVLCPWGKKAFSGYLGT-DQSKWKAYDATHLVKSYPGsQLDILIDQGKDDQFLLDGQLlpdNFIAACTEKKIP 249
Cdd:COG0627 143 AFSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIP 218

                       250       260       270
                ....*....|....*....|....*....|..
gi 33413400 250 VVFRLQEGYdHSYYFIATFITDHIRHHAKYLN 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 1.83e-82

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: 248.14  E-value: 1.83e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    23 SVELNCKMKFAVYLP-PKAETGKCPALYWLSGlTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGeDESWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   102 gagfyVDATEDPWKTNYRmySYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   182 PWGKkafsgylgTDQSKWKAYDATHLVK--SYPGSQLDILIDQGKDDQFLLDgQLLPDNFIAACTEKKIP--VVFRLQEG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAValSANNTRLRIYLDVGTREDFLGD-QLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 33413400   258 YDHSY-------YFIATFITDHIRH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
22-262 3.18e-20

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 88.37  E-value: 3.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  22 DSVELNCKMKFAVYLPP--KAETGKCPALYWLSGLTCTEQNFISKSGYHQSA----SEHGL---VVIAPDtsprgcNIKG 92
Cdd:COG2382  87 PSKALGRTRRVWVYLPPgyDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPD------GGDG 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  93 EDESWDFGTGAGFyvdatedpwktnyrmYSYVTEELPQLINANFPV--DPQRMSIFGHSMGGHGALICALKNPGKYKSVS 170
Cdd:COG2382 161 GDRGTEGPGNDAF---------------ERFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVG 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 171 afapicnpvlcpwgkkAFSGYLGTDQSKWKAYDATHLVK-SYPGSQLDILIDQGKDDQFLLDGQllpdNFIAACTEKKIP 249
Cdd:COG2382 226 ----------------SFSGSFWWPPGDADRGGWAELLAaGAPKKPLRFYLDVGTEDDLLEANR----ALAAALKAKGYD 285

                       250
                ....*....|...
gi 33413400 250 VVFRLQEGyDHSY 262
Cdd:COG2382 286 VEYREFPG-GHDW 297
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-278 1.59e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 62.73  E-value: 1.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  34 VYLPPKAetGKCPALYWLSGLTCTEQNFISksGYHQSASEHGLVVIAPDtsPRGC----NIKGEDESWDFGTGAGFyvdA 109
Cdd:COG1506  14 LYLPADG--KKYPVVVYVHGGPGSRDDSFL--PLAQALASRGYAVLAPD--YRGYgesaGDWGGDEVDDVLAAIDY---L 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 110 TEDPWktnyrmysyvteelpqlinanfpVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPV----LCPWGK 185
Cdd:COG1506  85 AARPY-----------------------VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRsyygTTREYT 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 186 KAFSGYLGTDQSKWKAYDATHLVKSYPGsqlDILIDQGKDDQFLLDGQLlpDNFIAACTEKKIPVVFRLQEGYDHSYYFI 265
Cdd:COG1506 142 ERLMGGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQA--ERLYEALKKAGKPVELLVYPGEGHGFSGA 216

                       250
                ....*....|....*...
gi 33413400 266 ATF-----ITDHIRHHAK 278
Cdd:COG1506 217 GAPdylerILDFLDRHLK 234
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
34-261 1.11e-07

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 51.52  E-value: 1.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  34 VYLPP--KAETGKCPALYWLSGltctEQNFISKSGYHQSASEHG-----LVVIA----PDTSPR-----GCNIKGEDESW 97
Cdd:COG2819  25 VYLPPgyDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGigngDDGERRlrdytPPPAPGYPGPG 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  98 DFGTGAGFYVDatedpwktnyrmysYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYksvSAFApicn 177
Cdd:COG2819 101 GPGGGADAFLR--------------FLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLF---GRYI---- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400 178 pvlcpwgkkAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILI---DQGKDDQFLLDGQLLpDNFIAACTEKKIPVVFRL 254
Cdd:COG2819 160 ---------AISPSLWWDDGALLDEAEALLKRSPLPKRLYLSVgtlEGDSMDGMVDDARRL-AEALKAKGYPGLNVKFEV 229


                ....*..
gi 33413400 255 QEGYDHS 261
Cdd:COG2819 230 FPGETHG 236
COG4099 COG4099
Predicted peptidase [General function prediction only];
30-176 1.96e-07

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 50.74  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  30 MKFAVYLPPKAETG-KCPALYWLSG-----------LTCTEQNFISKsgyhQSASEHGLVVIAPDTSprgcnikgEDESW 97
Cdd:COG4099  33 LPYRLYLPKGYDPGkKYPLVLFLHGagergtdnekqLTHGAPKFINP----ENQAKFPAIVLAPQCP--------EDDYW 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33413400  98 DFGTgagfYVDATEDpwktnyrMYSYVTeelpqlinANFPVDPQRMSIFGHSMGGHGALICALKNPGKYksvSAFAPIC 176
Cdd:COG4099 101 SDTK----ALDAVLA-------LLDDLI--------AEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPIC 157
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
69-263 9.87e-07

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 48.38  E-value: 9.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    69 QSASEHGLVVIAPDtsPRGCNIKGEDeswdfgtgagFYVDATEDpWKTNyrmysyvteELPQLINA------NFPVDPQR 142
Cdd:pfam00326   8 QLLADRGYVVAIAN--GRGSGGYGEA----------FHDAGKGD-LGQN---------EFDDFIAAaeylieQGYTDPDR 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   143 MSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVL-------------CPWGkkaFSGYLGTDQSKWKAYDATHLVK 209
Cdd:pfam00326  66 LAIWGGSYGGYLTGAALNQRPDLFKAAVAHVPVVDWLAymsdtslpfteryMEWG---NPWDNEEGYDYLSPYSPADNVK 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 33413400   210 SYPgsqlDILIDQGkddqfLLDGQLLPDN---FIAACTEKKIPVVFRLQEGYDHSYY 263
Cdd:pfam00326 143 VYP----PLLLIHG-----LLDDRVPPWQslkLVAALQRKGVPFLLLIFPDEGHGIG 190
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 32-173 2.73e-06

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 47.69  E-value: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  32 FAVYLPPKAETGK-CPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIkgedeSWDFGTG-------- 102
Cdd:COG3509  39 YRLYVPAGYDGGApLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGR-----CWNWFDGrdqrrgrd 113

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33413400 103 -AGFYVDATEDpwktnyrmysyvteelpqlINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFA 173
Cdd:COG3509 114 dVAFIAALVDD-------------------LAARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
73-159 8.48e-04

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 40.09  E-value: 8.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  73 EHGLVVIAPDTSprgcnikGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELpQLINANFP-----VDPQRMSIFG 147
Cdd:COG4188  87 SHGYVVAAPDHP-------GSNAADLSAALDGLADALDPEELWERPLDLSFVLDQL-LALNKSDPplagrLDLDRIGVIG 158

                        90
                ....*....|..
gi 33413400 148 HSMGGHGALICA 159
Cdd:COG4188 159 HSLGGYTALALA 170
AXE1 pfam05448
Acetyl xylan esterase (AXE1); This family consists of several bacterial acetyl xylan esterase ...
 33-177 3.98e-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: 38.15  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400    33 AVYLPPKAETGKCPALYwlsgltcteqNFIsksGYHQSASE---------HGLVVIAPDTspRGCNIKGEDESWDF--GT 101
Cdd:pfam05448  70 AWYVVPKESEEKHPAVV----------HFH---GYNGRRGDwhdmlhwaaHGYAVFVMDV--RGQGGLSEDDPRGPkgNT 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400   102 GAGFYVDATEDPWKTNYRmysYVTEELPQLIN--ANFP-VDPQRMSIFGHSMGGHGALICALKNPgKYKSVSAFAP-ICN 177
Cdd:pfam05448 135 YKGHITRGLLDRETYYYR---RVFLDAVRAVEivMSFPeVDEERIVVTGGSQGGALALAAAALSP-RIKAVVADYPfLSD 210
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 34-156 5.66e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 37.59  E-value: 5.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33413400  34 VYLPPKAEtGKCPALYWLSGLTcteQNFISKSGYHQSASEHGLVVIAPDtsPRGCnikGEDEswdfgtgaGFYVDAtEDP 113
Cdd:COG1073  27 LYLPAGAS-KKYPAVVVAHGNG---GVKEQRALYAQRLAELGFNVLAFD--YRGY---GESE--------GEPREE-GSP 88

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 33413400 114 WKTNYR-MYSYVTEeLPQlinanfpVDPQRMSIFGHSMGGHGAL 156
Cdd:COG1073  89 ERRDARaAVDYLRT-LPG-------VDPERIGLLGISLGGGYAL 124
 
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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