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Conserved domains on  [gi|961011235|ref|XP_014821735|]
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PREDICTED: S-formylglutathione hydrolase [Calidris pugnax]

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, ...
 2-281 1.75e-159

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: 444.99  E-value: 1.75e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   2 ALKQVSSNKCFEGFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  82 DTSPRGCNIEGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYIKDELPKLINANFPT-DPERMSVFGHSMGGHGALILAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDQlDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 161 KNPGKYKSVSAFAPICNPIQCQWGKKALGGYLGSDVSKWEAYDATQLVKSYPDSHLDILIDQGKDDQFLsAGQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFL-KEQLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 961011235 241 AACTERKIPVVFRLQQGYDHSYFFIATFINDHIKHHAKYLN 281
Cdd:PLN02442 242 EACKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQALK 282
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 1.75e-159

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 444.99  E-value: 1.75e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   2 ALKQVSSNKCFEGFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  82 DTSPRGCNIEGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYIKDELPKLINANFPT-DPERMSVFGHSMGGHGALILAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDQlDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 161 KNPGKYKSVSAFAPICNPIQCQWGKKALGGYLGSDVSKWEAYDATQLVKSYPDSHLDILIDQGKDDQFLsAGQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFL-KEQLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 961011235 241 AACTERKIPVVFRLQQGYDHSYFFIATFINDHIKHHAKYLN 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 7.62e-149

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: 417.64  E-value: 7.62e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235    6 VSSNKCFEGFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   86 RGCNIEGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYIKDELPKLINANFPTDPERMSVFGHSMGGHGALILALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  166 YKSVSAFAPICNPIQCQWGKKALGGYLGSDVSKWEAYDATQLVKSYpDSHLDILIDQGKDDQFLsAGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQFL-DEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 961011235  246 RKIPVVFRLQQGYDHSYFFIATFINDHIKHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
14-281 1.27e-109

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 317.16  E-value: 1.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  14 GFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAPDtsprgcniege 93
Cdd:COG0627    2 GRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  94 deswdfGTGAGFYVDATEDPWKtNYRMYSYIKDELPKLINANFPTDP--ERMSVFGHSMGGHGALILALKNPGKYKSVSA 171
Cdd:COG0627   71 ------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSAdrERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 172 FAPICNPIQCQWGKKALGGYLGS-DVSKWEAYDATQLVKSYPDsHLDILIDQGKDDQFLSAGQLlpdNFIAACTERKIPV 250
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIPH 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 961011235 251 VFRLQQGYdHSYFFIATFINDHIKHHAKYLN 281
Cdd:COG0627  220 TYRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 23-275 1.47e-76

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: 233.12  E-value: 1.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   23 SAELKCKMKFGIYLP-PKAETAKCPVLYWLSGlTCTEQNFITKAGFHQAAAEHGLIVVAPDTSPRGCNIEGeDESWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  102 gagfyVDATEDPWKTNYRmySYIKDELPKLINANFPTDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFAPICNPIQC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  182 QWGKkalggylgSDVSKWEAYDATQLVKSYPDS--HLDILIDQGKDDQFLsAGQLLPDNFIAACTERKIP--VVFRLQQG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAVALSANntRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 961011235  258 YDHSY-------FFIATFINDHIKH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
PLN02442 PLN02442
S-formylglutathione hydrolase
 2-281 1.75e-159

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 444.99  E-value: 1.75e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   2 ALKQVSSNKCFEGFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAP 81
Cdd:PLN02442   4 ALKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  82 DTSPRGCNIEGEDESWDFGTGAGFYVDATEDPWKtNYRMYSYIKDELPKLINANFPT-DPERMSVFGHSMGGHGALILAL 160
Cdd:PLN02442  84 DTSPRGLNVEGEADSWDFGVGAGFYLNATQEKWK-NWRMYDYVVKELPKLLSDNFDQlDTSRASIFGHSMGGHGALTIYL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 161 KNPGKYKSVSAFAPICNPIQCQWGKKALGGYLGSDVSKWEAYDATQLVKSYPDSHLDILIDQGKDDQFLsAGQLLPDNFI 240
Cdd:PLN02442 163 KNPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDVSATILIDQGEADKFL-KEQLLPENFE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 961011235 241 AACTERKIPVVFRLQQGYDHSYFFIATFINDHIKHHAKYLN 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 7.62e-149

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: 417.64  E-value: 7.62e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235    6 VSSNKCFEGFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAPDTSP 85
Cdd:TIGR02821   3 ISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDTSP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   86 RGCNIEGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYIKDELPKLINANFPTDPERMSVFGHSMGGHGALILALKNPGK 165
Cdd:TIGR02821  83 RGTGIAGEDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERQGITGHSMGGHGALVIALKNPDR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  166 YKSVSAFAPICNPIQCQWGKKALGGYLGSDVSKWEAYDATQLVKSYpDSHLDILIDQGKDDQFLsAGQLLPDNFIAACTE 245
Cdd:TIGR02821 163 FKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADG-GRHSTILIDQGTADQFL-DEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 961011235  246 RKIPVVFRLQQGYDHSYFFIATFINDHIKHHAKYL 280
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
14-281 1.27e-109

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 317.16  E-value: 1.27e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  14 GFQKVFEHDSAELKCKMKFGIYLPPKAETAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAPDtsprgcniege 93
Cdd:COG0627    2 GRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  94 deswdfGTGAGFYVDATEDPWKtNYRMYSYIKDELPKLINANFPTDP--ERMSVFGHSMGGHGALILALKNPGKYKSVSA 171
Cdd:COG0627   71 ------GGQASFYVDWTQGPAG-HYRWETYLTEELPPLIEANFPVSAdrERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 172 FAPICNPIQCQWGKKALGGYLGS-DVSKWEAYDATQLVKSYPDsHLDILIDQGKDDQFLSAGQLlpdNFIAACTERKIPV 250
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRA-GLPLYIDCGTADPFFLEANR---QLHAALRAAGIPH 219

                        250       260       270
                 ....*....|....*....|....*....|.
gi 961011235 251 VFRLQQGYdHSYFFIATFINDHIKHHAKYLN 281
Cdd:COG0627  220 TYRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 23-275 1.47e-76

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: 233.12  E-value: 1.47e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   23 SAELKCKMKFGIYLP-PKAETAKCPVLYWLSGlTCTEQNFITKAGFHQAAAEHGLIVVAPDTSPRGCNIEGeDESWDFGt 101
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSF-YSDWDRG- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  102 gagfyVDATEDPWKTNYRmySYIKDELPKLINANFPTDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFAPICNPIQC 181
Cdd:pfam00756  78 -----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNS 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  182 QWGKkalggylgSDVSKWEAYDATQLVKSYPDS--HLDILIDQGKDDQFLsAGQLLPDNFIAACTERKIP--VVFRLQQG 257
Cdd:pfam00756 151 MWGP--------EDDPAWQEGDPVLLAVALSANntRLRIYLDVGTREDFL-GDQLPVEILEELAPNRELAeqLAYRGVGG 221

                         250       260
                  ....*....|....*....|....*
gi 961011235  258 YDHSY-------FFIATFINDHIKH 275
Cdd:pfam00756 222 YDHEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
22-262 9.04e-24

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 98.00  E-value: 9.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  22 DSAELKCKMKFGIYLPP--KAETAKCPVLYWLSGLTCTEQNFITKAGFHQAA----AEHGL---IVVAPDtsprgcNIEG 92
Cdd:COG2382   87 PSKALGRTRRVWVYLPPgyDNPGKKYPVLYLLDGGGGDEQDWFDQGRLPTILdnliAAGKIppmIVVMPD------GGDG 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  93 EDESWDFGTGAGFYvdatedpwktnyrmySYIKDELPKLINANFPT--DPERMSVFGHSMGGHGALILALKNPGKYKSVS 170
Cdd:COG2382  161 GDRGTEGPGNDAFE---------------RFLAEELIPFVEKNYRVsaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVG 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 171 AFApicnpiqcqwgkkalgGYLGSDVSKWEAYDATQLVKSYPD-SHLDILIDQGKDDQFLSAGQllpdNFIAACTERKIP 249
Cdd:COG2382  226 SFS----------------GSFWWPPGDADRGGWAELLAAGAPkKPLRFYLDVGTEDDLLEANR----ALAAALKAKGYD 285

                        250
                 ....*....|...
gi 961011235 250 VVFRLQQGyDHSY 262
Cdd:COG2382  286 VEYREFPG-GHDW 297
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
34-262 1.45e-11

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 62.73  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  34 IYLPPKAEtaKCPVLYWLSGLTCTEQNFItkAGFHQAAAEHGLIVVAPDtsPRGCnieGEDESwDFGTGAgfYVDATedp 113
Cdd:COG1506   14 LYLPADGK--KYPVVVYVHGGPGSRDDSF--LPLAQALASRGYAVLAPD--YRGY---GESAG-DWGGDE--VDDVL--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 114 wktnyRMYSYIKDElPKLinanfptDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFAPICNPI----QCQWGKKALG 189
Cdd:COG1506   79 -----AAIDYLAAR-PYV-------DPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRsyygTTREYTERLM 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 961011235 190 GYLGSDVSKWEAYDATQLVKSYPDshlDILIDQGKDDQFLSAGQLlpDNFIAACTERKIPVVFRLQQGYDHSY 262
Cdd:COG1506  146 GGPWEDPEAYAARSPLAYADKLKT---PLLLIHGEADDRVPPEQA--ERLYEALKKAGKPVELLVYPGEGHGF 213
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
34-174 7.04e-11

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 61.15  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  34 IYLPP--KAETAKCPVLYWLSGltctEQNFITKAGFHQAAAEHG-----LIVVAPdtsprGCNIEGEDESWDFGtgagFY 106
Cdd:COG2819   25 VYLPPgyDAPEKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGI-----GNGDDGERRLRDYT----PP 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 961011235 107 VDATEDPWKTNY----RMYSYIKDELPKLINANFPTDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFAP 174
Cdd:COG2819   92 PAPGYPGPGGPGggadAFLRFLEEELKPYIDKRYRTDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISP 163
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
 34-173 5.80e-10

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 58.86  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  34 IYLPPKAE-TAKCPVLYWLSGLTCTEQNFITKAGFHQAAAEHGLIVVAPDTSPRGCNIegedeSWDFGTGAGFYVDATEd 112
Cdd:COG3509   41 LYVPAGYDgGAPLPLVVALHGCGGSAADFAAGTGLNALADREGFIVVYPEGTGRAPGR-----CWNWFDGRDQRRGRDD- 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 961011235 113 pwktnyrmYSYIKDelpkLIN---ANFPTDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFA 173
Cdd:COG3509  115 --------VAFIAA----LVDdlaARYGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVA 166
COG4099 COG4099
Predicted peptidase [General function prediction only];
30-186 1.91e-09

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 56.51  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  30 MKFGIYLPPK-AETAKCPVLYWLSG-------LTCTEQNFITKAGFHQAAAEHGLIVVAPDTSprgcniegEDESWDFGT 101
Cdd:COG4099   33 LPYRLYLPKGyDPGKKYPLVLFLHGagergtdNEKQLTHGAPKFINPENQAKFPAIVLAPQCP--------EDDYWSDTK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 102 gagfYVDATEDpwktnyrMYSYIKdelpklinANFPTDPERMSVFGHSMGGHGALILALKNPGKYksvSAFAPIC---NP 178
Cdd:COG4099  105 ----ALDAVLA-------LLDDLI--------AEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLF---AAAVPICgggDP 162


                 ....*...
gi 961011235 179 IQCQWGKK 186
Cdd:COG4099  163 ANAANLKK 170
COG4188 COG4188
Predicted dienelactone hydrolase [General function prediction only];
72-195 1.24e-06

Predicted dienelactone hydrolase [General function prediction only];


Pssm-ID: 443342 [Multi-domain]  Cd Length: 326  Bit Score: 48.95  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  72 AEHGLIVVAPDTSprgcnieGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYIKDELPKLiNANFPT-----DPERMSVF 146
Cdd:COG4188   86 ASHGYVVAAPDHP-------GSNAADLSAALDGLADALDPEELWERPLDLSFVLDQLLAL-NKSDPPlagrlDLDRIGVI 157

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 961011235 147 GHSMGGHGALILAlknpGKYKSVSAFAPICNP---IQCQWGKKALGGYLGSD 195
Cdd:COG4188  158 GHSLGGYTALALA----GARLDFAALRQYCGKnpdLQCRALDLPRLAYDLRD 205
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
72-263 5.14e-05

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 43.42  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  72 AEHGLIVVAPDTsprgcniEGEDESWDFGTGAGFYVDATeDPWKTNYRMYSYIkDELpklinANFP-TDPERMSVFGHSM 150
Cdd:COG0412   53 AAAGYVVLAPDL-------YGRGGPGDDPDEARALMGAL-DPELLAADLRAAL-DWL-----KAQPeVDAGRVGVVGFCF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235 151 GGHGALILALKNPGkYKSVSAFAPICnpiqcqwgkkalggylgsdvskweayDATQLVKSYPDSHLDILIDQGKDDQFLS 230
Cdd:COG0412  119 GGGLALLAAARGPD-LAAAVSFYGGL--------------------------PADDLLDLAARIKAPVLLLYGEKDPLVP 171

                        170       180       190
                 ....*....|....*....|....*....|...
gi 961011235 231 AGQLlpDNFIAACTERKIPVVFRLQQGYDHSYF 263
Cdd:COG0412  172 PEQV--AALEAALAAAGVDVELHVYPGAGHGFT 202
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 72-193 1.57e-03

Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.


Pssm-ID: 463473 [Multi-domain]  Cd Length: 238  Bit Score: 39.12  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235   72 AEHGLIVVAPDtsPRGcniegedeswdFGTGAGF--YVDATEDpwktnyrmysYIKD--ELPKLINANFPTDPerMSVFG 147
Cdd:pfam12146  28 AAQGFAVYAYD--HRG-----------HGRSDGKrgHVPSFDD----------YVDDldTFVDKIREEHPGLP--LFLLG 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 961011235  148 HSMGGHGALILALKNPGKYKSVSAFAPIC--NPIQCQWGKKALGGYLG 193
Cdd:pfam12146  83 HSMGGLIAALYALRYPDKVDGLILSAPALkiKPYLAPPILKLLAKLLG 130
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 138-174 3.37e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.39  E-value: 3.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 961011235 138 TDPERMSVFGHSMGGHGALILALKNPGKYKSVSAFAP 174
Cdd:PRK14875 194 LGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 72-173 4.05e-03

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 37.97  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 961011235  72 AEHGLIVVAPDtsPRGCnieGEDEswdfgtgaGFYVDAtEDPWKTNYR-MYSYIKdELPKLinanfptDPERMSVFGHSM 150
Cdd:COG1073   61 AELGFNVLAFD--YRGY---GESE--------GEPREE-GSPERRDARaAVDYLR-TLPGV-------DPERIGLLGISL 118

                         90       100
                 ....*....|....*....|....*
gi 961011235 151 GGHGALILA--LKNPGKYKSVSAFA 173
Cdd:COG1073  119 GGGYALNAAatDPRVKAVILDSPFT 143
 
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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