NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|488409109|ref|WP_002478494|]
View 

MULTISPECIES: alpha/beta hydrolase family protein [Staphylococcus]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11427881)

alpha/beta hydrolase family protein catalyzes the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787
PubMed:  19508187|12369917|37582413

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
4-250 9.77e-60

S-formylglutathione hydrolase FrmB [Defense mechanisms];


:

Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 189.27  E-value: 9.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   4 ITLNYQSPTIGMNQNLTVILPEDTSffksdgiAKPLKTVMLLHGLSSDATSYMRFTSIERYAESHQLAIIMPNA-DHSAY 82
Cdd:COG0627    5 VRVTVPSPALGREMPVSVYLPPGYD-------GRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPDGgQASFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  83 ANM----AYGHRYYDYIL-EVYHYVHQIFPLSTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFQaqtLIDLE 157
Cdd:COG0627   78 VDWtqgpAGHYRWETYLTeELPPLIEANFPVSADRERRAIAGLSMGGHGALTLALRHPDLFRAVAAFSGILD---PSQPP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 158 WTDYHPQAITGEHTNVKGTNLDTYHLVDAAVAReetlPELFIQCGTED-FLYQDNLTFIDYLADKQIPYRFEPSPGAHDY 236
Cdd:COG0627  155 WGEKAFDAYFGPPDRAAWAANDPLALAEKLRAG----LPLYIDCGTADpFFLEANRQLHAALRAAGIPHTYRERPGGHSW 230

                        250
                 ....*....|....
gi 488409109 237 TYWDKSIARALAWF 250
Cdd:COG0627  231 YYWASFLEDHLPFL 244
 
Name Accession Description Interval E-value
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
4-250 9.77e-60

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 189.27  E-value: 9.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   4 ITLNYQSPTIGMNQNLTVILPEDTSffksdgiAKPLKTVMLLHGLSSDATSYMRFTSIERYAESHQLAIIMPNA-DHSAY 82
Cdd:COG0627    5 VRVTVPSPALGREMPVSVYLPPGYD-------GRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPDGgQASFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  83 ANM----AYGHRYYDYIL-EVYHYVHQIFPLSTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFQaqtLIDLE 157
Cdd:COG0627   78 VDWtqgpAGHYRWETYLTeELPPLIEANFPVSADRERRAIAGLSMGGHGALTLALRHPDLFRAVAAFSGILD---PSQPP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 158 WTDYHPQAITGEHTNVKGTNLDTYHLVDAAVAReetlPELFIQCGTED-FLYQDNLTFIDYLADKQIPYRFEPSPGAHDY 236
Cdd:COG0627  155 WGEKAFDAYFGPPDRAAWAANDPLALAEKLRAG----LPLYIDCGTADpFFLEANRQLHAALRAAGIPHTYRERPGGHSW 230

                        250
                 ....*....|....
gi 488409109 237 TYWDKSIARALAWF 250
Cdd:COG0627  231 YYWASFLEDHLPFL 244
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 10-250 3.46e-13

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: 67.10  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   10 SPTIGMNQNLTVILPEDTSffksdgIAKPLKTVMLLHGlssdaTSYMRFTSI----ERYAESHQLA----IIMPNADHSA 81
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYP------PGRKYPVLYLLDG-----TGWFQNGPAkeglDRLAASGEIPpviiVGSPRGGEVS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   82 -YANMAYGHR---------YYDYIL-EVYHYVHQIFPlsTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqa 150
Cdd:pfam00756  70 fYSDWDRGLNategpgayaYETFLTqELPPLLDANFP--TAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPIL-- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  151 qtlidlewtdYHPQAITGEHTNVKGTNLDTYHLVDAAVAREETLPeLFIQCGTEDFLYQDNLT------------FIDYL 218
Cdd:pfam00756 146 ----------NPSNSMWGPEDDPAWQEGDPVLLAVALSANNTRLR-IYLDVGTREDFLGDQLPveileelapnreLAEQL 214

                         250       260       270
                  ....*....|....*....|....*....|..
gi 488409109  219 ADKQIPYRFEPSPGAHDYTYWDKSIARALAWF 250
Cdd:pfam00756 215 AYRGVGGYDHEYYGGHDWAYWRAQLIAALIDL 246
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 8-146 4.93e-05

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: 43.61  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109    8 YQSPTIGMNQNLTVILPEDTSffksdgiAKPLKTVMLLHGLSSDATSYMRFTSIERYAESHQLAIIMPN--------ADH 79
Cdd:TIGR02821  18 HKSETCGVPMTFGVFLPPQAA-------AGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDtsprgtgiAGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   80 SAYANMAYG---------------HRYYDYIL-EVYHYVHQIFPLSTRRedNFIAGHSMGGYGTMKFALTQSHLF---SK 140
Cdd:TIGR02821  91 DDAWDFGKGagfyvdateepwsqhYRMYSYIVqELPALVAAQFPLDGER--QGITGHSMGGHGALVIALKNPDRFksvSA 168


                  ....*.
gi 488409109  141 AAPMSA 146
Cdd:TIGR02821 169 FAPIVA 174
 
Name Accession Description Interval E-value
FrmB COG0627
S-formylglutathione hydrolase FrmB [Defense mechanisms];
4-250 9.77e-60

S-formylglutathione hydrolase FrmB [Defense mechanisms];


Pssm-ID: 440392 [Multi-domain]  Cd Length: 249  Bit Score: 189.27  E-value: 9.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   4 ITLNYQSPTIGMNQNLTVILPEDTSffksdgiAKPLKTVMLLHGLSSDATSYMRFTSIERYAESHQLAIIMPNA-DHSAY 82
Cdd:COG0627    5 VRVTVPSPALGREMPVSVYLPPGYD-------GRPLPVLYLLHGLTGTHENWTRKTGAQRLAAELGVIVVMPDGgQASFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  83 ANM----AYGHRYYDYIL-EVYHYVHQIFPLSTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFQaqtLIDLE 157
Cdd:COG0627   78 VDWtqgpAGHYRWETYLTeELPPLIEANFPVSADRERRAIAGLSMGGHGALTLALRHPDLFRAVAAFSGILD---PSQPP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 158 WTDYHPQAITGEHTNVKGTNLDTYHLVDAAVAReetlPELFIQCGTED-FLYQDNLTFIDYLADKQIPYRFEPSPGAHDY 236
Cdd:COG0627  155 WGEKAFDAYFGPPDRAAWAANDPLALAEKLRAG----LPLYIDCGTADpFFLEANRQLHAALRAAGIPHTYRERPGGHSW 230

                        250
                 ....*....|....
gi 488409109 237 TYWDKSIARALAWF 250
Cdd:COG0627  231 YYWASFLEDHLPFL 244
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
5-250 2.44e-32

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 120.34  E-value: 2.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   5 TLNYQSPTIGMNQNLTVILPEDTsffksDGIAKPLKTVMLLHGLSSDATSYMRF----TSIERYAESHQL---AIIMPNA 77
Cdd:COG2382   83 TVTYPSKALGRTRRVWVYLPPGY-----DNPGKKYPVLYLLDGGGGDEQDWFDQgrlpTILDNLIAAGKIppmIVVMPDG 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  78 DHSAYANMAYGH--RYYDYIL-EVYHYVHQIFPLSTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqaqtli 154
Cdd:COG2382  158 GDGGDRGTEGPGndAFERFLAeELIPFVEKNYRVSADPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSF------ 231

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 155 dleWTDYHPQAITGEHTNVkgtnldtyhlvdAAVAREETLPeLFIQCGTEDFLYQDNLTFIDYLADKQIPYRFEPSPGAH 234
Cdd:COG2382  232 ---WWPPGDADRGGWAELL------------AAGAPKKPLR-FYLDVGTEDDLLEANRALAAALKAKGYDVEYREFPGGH 295

                        250
                 ....*....|....*.
gi 488409109 235 DYTYWDKSIARALAWF 250
Cdd:COG2382  296 DWAVWRAALPDFLPWL 311
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
 10-250 3.46e-13

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: 67.10  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   10 SPTIGMNQNLTVILPEDTSffksdgIAKPLKTVMLLHGlssdaTSYMRFTSI----ERYAESHQLA----IIMPNADHSA 81
Cdd:pfam00756   1 SNSLGREMKVQVYLPEDYP------PGRKYPVLYLLDG-----TGWFQNGPAkeglDRLAASGEIPpviiVGSPRGGEVS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   82 -YANMAYGHR---------YYDYIL-EVYHYVHQIFPlsTRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqa 150
Cdd:pfam00756  70 fYSDWDRGLNategpgayaYETFLTqELPPLLDANFP--TAPDGRALAGQSMGGLGALYLALKYPDLFGSVSSFSPIL-- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  151 qtlidlewtdYHPQAITGEHTNVKGTNLDTYHLVDAAVAREETLPeLFIQCGTEDFLYQDNLT------------FIDYL 218
Cdd:pfam00756 146 ----------NPSNSMWGPEDDPAWQEGDPVLLAVALSANNTRLR-IYLDVGTREDFLGDQLPveileelapnreLAEQL 214

                         250       260       270
                  ....*....|....*....|....*....|..
gi 488409109  219 ADKQIPYRFEPSPGAHDYTYWDKSIARALAWF 250
Cdd:pfam00756 215 AYRGVGGYDHEYYGGHDWAYWRAQLIAALIDL 246
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
20-250 1.87e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 44.62  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  20 TVILPEDtsffksdgiAKPLKTVMLLHGlsSDATSYMRFTSIERYAESHQLAIIMPNADHSAYANMAYGHRYYDYILEVY 99
Cdd:COG1506   13 WLYLPAD---------GKKYPVVVYVHG--GPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDEVDDVLAAI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 100 HYVHQIFPLSTRRedNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqaqtliDLEWTDYHPQAITGEHTNVKGTNLD 179
Cdd:COG1506   82 DYLAARPYVDPDR--IGIYGHSYGGYMALLAAARHPDRFKAAVALAGVS------DLRSYYGTTREYTERLMGGPWEDPE 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409109 180 TYHLVD--AAVAREETlPELFIQcGTEDFL--YQDNLTFIDYLADKQIPYRFEPSPGA-HDYTYWD--KSIARALAWF 250
Cdd:COG1506  154 AYAARSplAYADKLKT-PLLLIH-GEADDRvpPEQAERLYEALKKAGKPVELLVYPGEgHGFSGAGapDYLERILDFL 229
fghA_ester_D TIGR02821
S-formylglutathione hydrolase; This model describes a protein family from bacteria, yeast, and ...
 8-146 4.93e-05

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: 43.61  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109    8 YQSPTIGMNQNLTVILPEDTSffksdgiAKPLKTVMLLHGLSSDATSYMRFTSIERYAESHQLAIIMPN--------ADH 79
Cdd:TIGR02821  18 HKSETCGVPMTFGVFLPPQAA-------AGPVPVLWYLSGLTCTHENFMIKAGAQRFAAEHGLALVAPDtsprgtgiAGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   80 SAYANMAYG---------------HRYYDYIL-EVYHYVHQIFPLSTRRedNFIAGHSMGGYGTMKFALTQSHLF---SK 140
Cdd:TIGR02821  91 DDAWDFGKGagfyvdateepwsqhYRMYSYIVqELPALVAAQFPLDGER--QGITGHSMGGHGALVIALKNPDRFksvSA 168


                  ....*.
gi 488409109  141 AAPMSA 146
Cdd:TIGR02821 169 FAPIVA 174
COG4099 COG4099
Predicted peptidase [General function prediction only];
3-146 7.67e-05

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 42.65  E-value: 7.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   3 YITLNYQSPTIGMNQNLTVILPEDTSffksDGIAKPLktVMLLHGLS---SDATSYM-----RFTSIERyAESHQLAIIM 74
Cdd:COG4099   19 FEARTFTDPSDGDTLPYRLYLPKGYD----PGKKYPL--VLFLHGAGergTDNEKQLthgapKFINPEN-QAKFPAIVLA 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409109  75 PNADHSAYANMAyghRYYDYILEVYHYVHQIFPLSTRREdnFIAGHSMGGYGTMKFALTQSHLFSKAAPMSA 146
Cdd:COG4099   92 PQCPEDDYWSDT---KALDAVLALLDDLIAEYRIDPDRI--YLTGLSMGGYGTWDLAARYPDLFAAAVPICG 158
YbbA COG2819
Predicted hydrolase of the alpha/beta superfamily [General function prediction only];
88-250 1.08e-04

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


Pssm-ID: 442067 [Multi-domain]  Cd Length: 250  Bit Score: 42.28  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  88 GHRYYDYIlevyhyVHQIFPL-----STRREDNFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqaqtlidleWtdYH 162
Cdd:COG2819  106 ADAFLRFL------EEELKPYidkryRTDPERTGLIGHSLGGLFSLYALLKYPDLFGRYIAISPSL---------W--WD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109 163 PQAITGEhtnvkgtnldtyhlVDAAVAREETLPELFIQCGTE-----DFLYQDNLTFIDYLADKQIP---YRFEPSPGA- 233
Cdd:COG2819  169 DGALLDE--------------AEALLKRSPLPKRLYLSVGTLegdsmDGMVDDARRLAEALKAKGYPglnVKFEVFPGEt 234

                        170
                 ....*....|....*..
gi 488409109 234 HDYTYWDkSIARALAWF 250
Cdd:COG2819  235 HGSVAWA-ALPRALRFL 250
YpfH COG0400
Predicted esterase [General function prediction only];
36-250 1.56e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  36 AKPLktVMLLHGLSSDATSymrFTSIERYAESHQLAIIMPNADHSAYANMAyghRYYD------------------YILE 97
Cdd:COG0400    4 AAPL--VVLLHGYGGDEED---LLPLAPELALPGAAVLAPRAPVPEGPGGR---AWFDlsflegredeeglaaaaeALAA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  98 VYHYVHQIFPLSTRREdnFIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFqaqtLIDLEWTDYHPQAitgEHTNVkgtn 177
Cdd:COG0400   76 FIDELEARYGIDPERI--VLAGFSQGAAMALSLALRRPELLAGVVALSGYL----PGEEALPAPEAAL---AGTPV---- 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409109 178 ldtyhlvdaavareetlpelFIQCGTED-FLYQDNL-TFIDYLADKQIPYRFEPSPGAHDYTywDKSIARALAWF 250
Cdd:COG0400  143 --------------------FLAHGTQDpVIPVERArEAAEALEAAGADVTYREYPGGHEIS--PEELADARAWL 195
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 36-144 4.87e-04

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: 40.28  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109   36 AKPLKTVMLLHGLSSdatsymrftSIERYAEshqLAIIMPNADHSAYANMAYGH--------------RYYDYILEVYHY 101
Cdd:pfam12146   1 GEPRAVVVLVHGLGE---------HSGRYAH---LADALAAQGFAVYAYDHRGHgrsdgkrghvpsfdDYVDDLDTFVDK 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488409109  102 VHQIFPLSTRrednFIAGHSMGGYGTMKFALTQSHLFSKA---APM 144
Cdd:pfam12146  69 IREEHPGLPL----FLLGHSMGGLIAALYALRYPDKVDGLilsAPA 110
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 40-150 9.02e-04

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: 39.60  E-value: 9.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  40 KTVMLLHGLSSDATSYMRFtsIERYAESHQ-LAIIMPNADHSAYANMAYG-HRYYDYILEVyhyvhqifpLSTRREDNFI 117
Cdd:COG0596   24 PPVVLLHGLPGSSYEWRPL--IPALAAGYRvIAPDLRGHGRSDKPAGGYTlDDLADDLAAL---------LDALGLERVV 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488409109 118 -AGHSMGGYGTMKFALTQSHLFSKAAPMSAVFQA 150
Cdd:COG0596   93 lVGHSMGGMVALELAARHPERVAGLVLVDEVLAA 126
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
36-154 4.13e-03

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 37.29  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409109  36 AKPLKTVMLLHGLSSDATSYMRFtsIERYAEsHQLAIIMPnaDHSAY----ANMAYGHRYYDYILEVYHYVHQIfplstR 111
Cdd:COG2267   25 GSPRGTVVLVHGLGEHSGRYAEL--AEALAA-AGYAVLAF--DLRGHgrsdGPRGHVDSFDDYVDDLRAALDAL-----R 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488409109 112 REDN---FIAGHSMGGYGTMKFALTQSHLFSKAAPMSAVFQAQTLI 154
Cdd:COG2267   95 ARPGlpvVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLL 140
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH