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Conserved domains on  [gi|896507809|ref|WP_049415264|]
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S-formylglutathione hydrolase [Stenotrophomonas maltophilia]

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, ...
 2-274 2.53e-149

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 TIGR02821:

Pssm-ID: 473884  Cd Length: 275  Bit Score: 418.41  E-value: 2.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809    2 ERIEHRACFGGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   82 SPRGDDVAD-AEGYDLGKGAGFYLNATRAPWAKHYRMHDYVAQELPTLIEANFPVTGAR-AVSGHSMGGHGALVIALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERqGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  160 GRYRSVSAFSPIVAPSHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASERLPLLVDQGEADEFLQTQLQPQRLQEACAA 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 896507809  240 AGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARAL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-274 2.53e-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: 418.41  E-value: 2.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809    2 ERIEHRACFGGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   82 SPRGDDVAD-AEGYDLGKGAGFYLNATRAPWAKHYRMHDYVAQELPTLIEANFPVTGAR-AVSGHSMGGHGALVIALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERqGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  160 GRYRSVSAFSPIVAPSHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASERLPLLVDQGEADEFLQTQLQPQRLQEACAA 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 896507809  240 AGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARAL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 1-274 2.61e-147

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 413.79  E-value: 2.61e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   1 MERIEHRACFGGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPD 80
Cdd:PLN02442   5 LKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  81 TSPRGDDV-ADAEGYDLGKGAGFYLNATRAPWaKHYRMHDYVAQELPTLIEANFPV--TGARAVSGHSMGGHGALVIALR 157
Cdd:PLN02442  85 TSPRGLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQldTSRASIFGHSMGGHGALTIYLK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 158 NPGRYRSVSAFSPIVAPSHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASE-RLPLLVDQGEADEFLQTQLQPQRLQEA 236
Cdd:PLN02442 164 NPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDvSATILIDQGEADKFLKEQLLPENFEEA 243

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 896507809 237 CAAAGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARAL 274
Cdd:PLN02442 244 CKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
11-275 1.34e-119

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 342.20  E-value: 1.34e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  11 GGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPDtsprgddvad 90
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  91 aegydlGKGAGFYLNATRAPwAKHYRMHDYVAQELPTLIEANFPV---TGARAVSGHSMGGHGALVIALRNPGRYRSVSA 167
Cdd:COG0627   71 ------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVsadRERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 168 FSPIVAPSHVPWGQKAFTAYLGD-NPADWAQWDTCALLEAASERLPLLVDQGEADE-FLQTQLQpqrLQEACAAAGHPLT 245
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGLPLYIDCGTADPfFLEANRQ---LHAALRAAGIPHT 220

                        250       260       270
                 ....*....|....*....|....*....|
gi 896507809 246 LRLQPGYdHSYYFIASFIGEHIAHHARALH 275
Cdd:COG0627  221 YRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-269 1.47e-67

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: 210.01  E-value: 1.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   21 STTLGCDMQFAVYLP-PQAEVQPLPVLYWLSGlTCTEQNFITKAGAQRYAAEHGVIIVAPDTSPRGDDVADAEGYDLGkg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  100 agfyLNATRAPWAKHYRmhDYVAQELPTLIEANFPVTG-ARAVSGHSMGGHGALVIALRNPGRYRSVSAFSPIVAPSHVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPdGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  179 WGQKaftaylgDNPAdWAQWDTCALLEAAS---ERLPLLVDQGEADEFLQTQLQPQRLQEACAAAGHP--LTLRLQPGYD 253
Cdd:pfam00756 152 WGPE-------DDPA-WQEGDPVLLAVALSannTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGGYD 223

                         250       260
                  ....*....|....*....|...
gi 896507809  254 HSY-------YFIASFIGEHIAH 269
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
 
Name Accession Description Interval E-value
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 2-274 2.53e-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: 418.41  E-value: 2.53e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809    2 ERIEHRACFGGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPDT 81
Cdd:TIGR02821   1 ELISSHACFGGTQGFYRHKSETCGVPMTFGVFLPPQAAAGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   82 SPRGDDVAD-AEGYDLGKGAGFYLNATRAPWAKHYRMHDYVAQELPTLIEANFPVTGAR-AVSGHSMGGHGALVIALRNP 159
Cdd:TIGR02821  81 SPRGTGIAGeDDAWDFGKGAGFYVDATEEPWSQHYRMYSYIVQELPALVAAQFPLDGERqGITGHSMGGHGALVIALKNP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  160 GRYRSVSAFSPIVAPSHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASERLPLLVDQGEADEFLQTQLQPQRLQEACAA 239
Cdd:TIGR02821 161 DRFKSVSAFAPIVAPSRCPWGQKAFSAYLGADEAAWRSYDASLLVADGGRHSTILIDQGTADQFLDEQLRPDAFEQACRA 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 896507809  240 AGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARAL 274
Cdd:TIGR02821 241 AGQALTLRRQAGYDHSYYFIASFIADHLRHHAERL 275
PLN02442 PLN02442
S-formylglutathione hydrolase
 1-274 2.61e-147

S-formylglutathione hydrolase


Pssm-ID: 178061 [Multi-domain]  Cd Length: 283  Bit Score: 413.79  E-value: 2.61e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   1 MERIEHRACFGGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPD 80
Cdd:PLN02442   5 LKEISVNKMFGGFNRRYKHFSSTLGCSMTFSVYFPPASDSGKVPVLYWLSGLTCTDENFIQKSGAQRAAAARGIALVAPD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  81 TSPRGDDV-ADAEGYDLGKGAGFYLNATRAPWaKHYRMHDYVAQELPTLIEANFPV--TGARAVSGHSMGGHGALVIALR 157
Cdd:PLN02442  85 TSPRGLNVeGEADSWDFGVGAGFYLNATQEKW-KNWRMYDYVVKELPKLLSDNFDQldTSRASIFGHSMGGHGALTIYLK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 158 NPGRYRSVSAFSPIVAPSHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASE-RLPLLVDQGEADEFLQTQLQPQRLQEA 236
Cdd:PLN02442 164 NPDKYKSVSAFAPIANPINCPWGQKAFTNYLGSDKADWEEYDATELVSKFNDvSATILIDQGEADKFLKEQLLPENFEEA 243

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 896507809 237 CAAAGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARAL 274
Cdd:PLN02442 244 CKEAGAPVTLRLQPGYDHSYFFIATFIDDHINHHAQAL 281
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
11-275 1.34e-119

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 342.20  E-value: 1.34e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  11 GGWQDVYRHRSTTLGCDMQFAVYLPPQAEVQPLPVLYWLSGLTCTEQNFITKAGAQRYAAEHGVIIVAPDtsprgddvad 90
Cdd:COG0627    1 GGRVVRVTVPSPALGREMPVSVYLPPGYDGRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPD---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  91 aegydlGKGAGFYLNATRAPwAKHYRMHDYVAQELPTLIEANFPV---TGARAVSGHSMGGHGALVIALRNPGRYRSVSA 167
Cdd:COG0627   71 ------GGQASFYVDWTQGP-AGHYRWETYLTEELPPLIEANFPVsadRERRAIAGLSMGGHGALTLALRHPDLFRAVAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 168 FSPIVAPSHVPWGQKAFTAYLGD-NPADWAQWDTCALLEAASERLPLLVDQGEADE-FLQTQLQpqrLQEACAAAGHPLT 245
Cdd:COG0627  144 FSGILDPSQPPWGEKAFDAYFGPpDRAAWAANDPLALAEKLRAGLPLYIDCGTADPfFLEANRQ---LHAALRAAGIPHT 220

                        250       260       270
                 ....*....|....*....|....*....|
gi 896507809 246 LRLQPGYdHSYYFIASFIGEHIAHHARALH 275
Cdd:COG0627  221 YRERPGG-HSWYYWASFLEDHLPFLARALG 249
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 21-269 1.47e-67

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: 210.01  E-value: 1.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   21 STTLGCDMQFAVYLP-PQAEVQPLPVLYWLSGlTCTEQNFITKAGAQRYAAEHGVIIVAPDTSPRGDDVADAEGYDLGkg 99
Cdd:pfam00756   1 SNSLGREMKVQVYLPeDYPPGRKYPVLYLLDG-TGWFQNGPAKEGLDRLAASGEIPPVIIVGSPRGGEVSFYSDWDRG-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  100 agfyLNATRAPWAKHYRmhDYVAQELPTLIEANFPVTG-ARAVSGHSMGGHGALVIALRNPGRYRSVSAFSPIVAPSHVP 178
Cdd:pfam00756  78 ----LNATEGPGAYAYE--TFLTQELPPLLDANFPTAPdGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPILNPSNSM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  179 WGQKaftaylgDNPAdWAQWDTCALLEAAS---ERLPLLVDQGEADEFLQTQLQPQRLQEACAAAGHP--LTLRLQPGYD 253
Cdd:pfam00756 152 WGPE-------DDPA-WQEGDPVLLAVALSannTRLRIYLDVGTREDFLGDQLPVEILEELAPNRELAeqLAYRGVGGYD 223

                         250       260
                  ....*....|....*....|...
gi 896507809  254 HSY-------YFIASFIGEHIAH 269
Cdd:pfam00756 224 HEYygghdwaYWRAQLIAALIDL 246
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
20-256 8.83e-26

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 103.39  E-value: 8.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  20 RSTTLGCDMQFAVYLPPQAEV--QPLPVLYWLSGLTCTEQNFITKAGAQR----YAAEHGV---IIVAPDTSPRGDdvad 90
Cdd:COG2382   87 PSKALGRTRRVWVYLPPGYDNpgKKYPVLYLLDGGGGDEQDWFDQGRLPTildnLIAAGKIppmIVVMPDGGDGGD---- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  91 aEGYDLGKGAGFYlnatrapwakhyrmhDYVAQELPTLIEANFPVT---GARAVSGHSMGGHGALVIALRNPGRYRSVSA 167
Cdd:COG2382  163 -RGTEGPGNDAFE---------------RFLAEELIPFVEKNYRVSadpEHRAIAGLSMGGLAALYAALRHPDLFGYVGS 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 168 FSPivapshvpwgqkaftaYLGDNPADWAQWDTCALLEAASER--LPLLVDQGEADEFLQtqlQPQRLQEACAAAGHPLT 245
Cdd:COG2382  227 FSG----------------SFWWPPGDADRGGWAELLAAGAPKkpLRFYLDVGTEDDLLE---ANRALAAALKAKGYDVE 287

                        250
                 ....*....|.
gi 896507809 246 LRLQPGyDHSY 256
Cdd:COG2382  288 YREFPG-GHDW 297
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
20-262 9.87e-12

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 63.47  E-value: 9.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  20 RSTTLGCDMQFAVYLPPQAEV--QPLPVLYWLSGltctEQNFITKAGAQRYAAEHG-----VIIVA----PDTSPRGDD- 87
Cdd:COG2819   13 ESPILGEDRRIRVYLPPGYDApeKRYPVLYMLDG----QNLFDALAGAVGTLSRLEggippAIVVGigngDDGERRLRDy 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  88 ---VADAEGYDLGKGAGfylnatrapwAKHYRmhDYVAQELPTLIEANFPVTGA-RAVSGHSMGGHGALVIALRNPGRYR 163
Cdd:COG2819   89 tppPAPGYPGPGGPGGG----------ADAFL--RFLEEELKPYIDKRYRTDPErTGLIGHSLGGLFSLYALLKYPDLFG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 164 SVSAFSPivapsHVPWGQKAFTAYLGDNPADWAQWDTCALLEAASERLPLLVDQGEADEFLqtqlqpQRLQEAcAAAGHP 243
Cdd:COG2819  157 RYIAISP-----SLWWDDGALLDEAEALLKRSPLPKRLYLSVGTLEGDSMDGMVDDARRLA------EALKAK-GYPGLN 224

                        250
                 ....*....|....*....
gi 896507809 244 LTLRLQPGYDHSYYFIASF 262
Cdd:COG2819  225 VKFEVFPGETHGSVAWAAL 243
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
25-257 1.21e-10

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 60.03  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  25 GCDMQFAVYLPPQAEvqPLPVLYWLSGLTCTeQNFITKAGAQRYAAeHGVIIVAPDtsPRGDdvadaeGYDLGKGAGFYL 104
Cdd:COG1506    7 GTTLPGWLYLPADGK--KYPVVVYVHGGPGS-RDDSFLPLAQALAS-RGYAVLAPD--YRGY------GESAGDWGGDEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 105 NATRApWAKHYRMHDYVAqelptlieanfpvtGAR-AVSGHSMGGHGALVIALRNPGRYRSVSAFSPIVAPSHVPWGQKA 183
Cdd:COG1506   75 DDVLA-AIDYLAARPYVD--------------PDRiGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTRE 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896507809 184 FTAYLGDNPADWAQ--WDTCALLEAASERLPLLVDQGEADEFLQTQlQPQRLQEACAAAGHPLTLRLQPGYDHSYY 257
Cdd:COG1506  140 YTERLMGGPWEDPEayAARSPLAYADKLKTPLLLIHGEADDRVPPE-QAERLYEALKKAGKPVELLVYPGEGHGFS 214
PRK10566 PRK10566
esterase; Provisional
 123-254 8.01e-09

esterase; Provisional


Pssm-ID: 182555 [Multi-domain]  Cd Length: 249  Bit Score: 54.99  E-value: 8.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 123 QELPTL----IEANFpVTGAR-AVSGHSMGGHGALVIALRNP-----------GRYRSVSA--FSPIVAPShvPWGQKAF 184
Cdd:PRK10566  89 QEFPTLraaiREEGW-LLDDRlAVGGASMGGMTALGIMARHPwvkcvaslmgsGYFTSLARtlFPPLIPET--AAQQAEF 165

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896507809 185 TAYLgdnpADWAQWDTCALLEAASERlPLLVDQGEADEFLQTQlQPQRLQEACAAAG--HPLTLRLQPGYDH 254
Cdd:PRK10566 166 NNIV----APLAEWEVTHQLEQLADR-PLLLWHGLADDVVPAA-ESLRLQQALRERGldKNLTCLWEPGVRH 231
COG4099 COG4099
Predicted peptidase [General function prediction only];
27-179 8.87e-04

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 39.57  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  27 DMQFAVYLPPQAEV-QPLPVLYWL--SGLTCTEQNFITKAGAQRYA-----AEHGVIIVAPdTSPRGDDvadaegydlgk 98
Cdd:COG4099   32 TLPYRLYLPKGYDPgKKYPLVLFLhgAGERGTDNEKQLTHGAPKFInpenqAKFPAIVLAP-QCPEDDY----------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809  99 gagfylnatrapWAKHYRMHDyvAQELPTLIEANFPVTGAR-AVSGHSMGGHGALVIALRNPGRYRSVSAFSPIVAPSHV 177
Cdd:COG4099  100 ------------WSDTKALDA--VLALLDDLIAEYRIDPDRiYLTGLSMGGYGTWDLAARYPDLFAAAVPICGGGDPANA 165


                 ..
gi 896507809 178 PW 179
Cdd:COG4099  166 AN 167
Chlorophyllase pfam07224
Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1. ...
 68-172 9.19e-04

Chlorophyllase; This family consists of several plant specific Chlorophyllase proteins (EC:3.1.1.14). Chlorophyllase (Chlase) is the first enzyme involved in chlorophyll (Chl) degradation and catalyzes the hydrolysis of ester bond to yield chlorophyllide and phytol.


Pssm-ID: 254111  Cd Length: 307  Bit Score: 40.21  E-value: 9.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809   68 YAAEHGVIIVAPDT-----SPRG-DDVADAegydlgkgagfylnATRAPWakhyrMHDYVAQELPTLIEANFPVTgarAV 141
Cdd:pfam07224  68 HIASHGFIVVAPQLyrlfpPPSQqDEIDSA--------------AEVANW-----LPLGLQVVLPTGVEANLSKL---AL 125

                          90       100       110
                  ....*....|....*....|....*....|.
gi 896507809  142 SGHSMGGHGALVIALrnpgRYRSVSAFSPIV 172
Cdd:pfam07224 126 SGHSRGGKTAFALAL----GYSLDVTFSALI 152
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
143-254 1.38e-03

Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 39.21  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 143 GHSMGGHGALVIALRNPGRYRSVSAFSPIVAPSHvpwgqkaftayLGDNPADWAqWDTCALLEAASERLPLLVDQGEADe 222
Cdd:COG2267  105 GHSMGGLIALLYAARYPDRVAGLVLLAPAYRADP-----------LLGPSARWL-RALRLAEALARIDVPVLVLHGGAD- 171

                         90       100       110
                 ....*....|....*....|....*....|..
gi 896507809 223 flqTQLQPQRLQEACAAAGHPLTLRLQPGYDH 254
Cdd:COG2267  172 ---RVVPPEAARRLAARLSPDVELVLLPGARH 200
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 143-170 1.96e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 39.16  E-value: 1.96e-03
                         10        20
                 ....*....|....*....|....*...
gi 896507809 143 GHSMGGHGALVIALRNPGRYRSVSAFSP 170
Cdd:PRK14875 203 GHSMGGAVALRLAARAPQRVASLTLIAP 230
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
140-273 2.56e-03

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 38.32  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896507809 140 AVSGHSMGGHGALVIALRNPGRYRS----VSAFSPIVAPSHVPwgqkaFTAYLGDNPadwaqwdtcalleaaserlPLLV 215
Cdd:COG0657   89 AVAGDSAGGHLAAALALRARDRGGPrpaaQVLIYPVLDLTASP-----LRADLAGLP-------------------PTLI 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 896507809 216 DQGEADEFLQtqlQPQRLQEACAAAGHPLTLRLQPGYDHSYYFIASFIGEHIAHHARA 273
Cdd:COG0657  145 VTGEADPLVD---ESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLPEARAALAEIA 199
 
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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