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Conserved domains on  [gi|504790830|ref|WP_014977932|]
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MULTISPECIES: alpha/beta hydrolase [Alteromonas]

Protein Classification

alpha/beta hydrolase( domain architecture ID 10785415)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
14-223 5.61e-73

Predicted esterase [General function prediction only];


:

Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 220.16  E-value: 5.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  14 STTPDACVIWLHGLGDSGHGFAPIVPELKLPEsmaVKFLFPHAPERPVtinggMRMRAWYDIKSLdfESRADLEGVKESA 93
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPG---AAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  94 AQVEALI-EAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDtNRETPIMMAHGEQ 172
Cdd:COG0400   71 EALAAFIdELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAA-LAGTPVFLAHGTQ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504790830 173 DEVVPVFMGNAAFKTLSESGFNATWQTYTMQHNVCMQELNDISAWLQKVLG 223
Cdd:COG0400  150 DPVIPVERAREAAEALEAAGADVTYREYPGGHEISPEELADARAWLAERLA 200
 
Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
14-223 5.61e-73

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 220.16  E-value: 5.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  14 STTPDACVIWLHGLGDSGHGFAPIVPELKLPEsmaVKFLFPHAPERPVtinggMRMRAWYDIKSLdfESRADLEGVKESA 93
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPG---AAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  94 AQVEALI-EAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDtNRETPIMMAHGEQ 172
Cdd:COG0400   71 EALAAFIdELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAA-LAGTPVFLAHGTQ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504790830 173 DEVVPVFMGNAAFKTLSESGFNATWQTYTMQHNVCMQELNDISAWLQKVLG 223
Cdd:COG0400  150 DPVIPVERAREAAEALEAAGADVTYREYPGGHEISPEELADARAWLAERLA 200
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
11-222 4.91e-59

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 185.27  E-value: 4.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   11 INPSTTPDACVIWLHGLGDSGHGFA-PIVPELKLPEsmaVKFLFPHAPERPVTINGGMRMRAWYDIKSLDFESRADLEGV 89
Cdd:pfam02230   7 VSPRDPAQATVIFLHGLGDSGHGWAdAAKTEAPLPN---IKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   90 KESAAQVEALIEAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDTNRETPIMMAH 169
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVTKKTPIFLIH 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504790830  170 GEQDEVVPVFMGNAAFKTLSESGFNATWQTYT-MQHNVCMQELNDISAWLQKVL 222
Cdd:pfam02230 164 GEEDPVVPLALGKLAKEYLKTSLNKVELKIYEgLAHSICGREMQDIKKFLSKHI 217
PRK11460 PRK11460
putative hydrolase; Provisional
12-196 2.93e-11

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 60.82  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  12 NPSTTPDACVIWLHGLGDSGHGFAPIVPELK--LPESMAVKflfPHAPErPVTINGGmrmRAWYDIKSLDFESRAdlegv 89
Cdd:PRK11460  10 SPDKPAQQLLLLFHGVGDNPVAMGEIGSWFApaFPDALVVS---VGGPE-PSGNGAG---RQWFSVQGITEDNRQ----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  90 KESAAQVEALIE----AQIESGIPSERIVLAGFSQGGVIALHlAPRYANKFAG-VIALS-TYMCEPsllgsEAKDTNreT 163
Cdd:PRK11460  78 ARVAAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMALE-AVKAEPGLAGrVIAFSgRYASLP-----ETAPTA--T 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 504790830 164 PIMMAHGEQDEVVPVFMGNAAFKTLSESGFNAT 196
Cdd:PRK11460 150 TIHLIHGGEDPVIDVAHAVAAQEALISLGGDVT 182
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
93-160 1.21e-04

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 42.23  E-value: 1.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504790830  93 AAQVEALIeAQIESGIPSeriVLAGFSQGGVIALHLAPRYANKFAGVIALstymcEPSLLGSEAKDTN 160
Cdd:cd12808  174 ALTLAAYD-ALLDRVGPC---IVVAHSQGGGFAFEAARARPDLVRAVVAL-----EPSGAPDPAEAAP 232
 
Name Accession Description Interval E-value
YpfH COG0400
Predicted esterase [General function prediction only];
14-223 5.61e-73

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 220.16  E-value: 5.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  14 STTPDACVIWLHGLGDSGHGFAPIVPELKLPEsmaVKFLFPHAPERPVtinggMRMRAWYDIKSLdfESRADLEGVKESA 93
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPG---AAVLAPRAPVPEG-----PGGRAWFDLSFL--EGREDEEGLAAAA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  94 AQVEALI-EAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDtNRETPIMMAHGEQ 172
Cdd:COG0400   71 EALAAFIdELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAA-LAGTPVFLAHGTQ 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504790830 173 DEVVPVFMGNAAFKTLSESGFNATWQTYTMQHNVCMQELNDISAWLQKVLG 223
Cdd:COG0400  150 DPVIPVERAREAAEALEAAGADVTYREYPGGHEISPEELADARAWLAERLA 200
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
11-222 4.91e-59

Phospholipase/Carboxylesterase; This family consists of both phospholipases and carboxylesterases with broad substrate specificity, and is structurally related to alpha/beta hydrolases pfam00561.


Pssm-ID: 396693 [Multi-domain]  Cd Length: 217  Bit Score: 185.27  E-value: 4.91e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   11 INPSTTPDACVIWLHGLGDSGHGFA-PIVPELKLPEsmaVKFLFPHAPERPVTINGGMRMRAWYDIKSLDFESRADLEGV 89
Cdd:pfam02230   7 VSPRDPAQATVIFLHGLGDSGHGWAdAAKTEAPLPN---IKFIFPHGPEIPVTLNGGMRMPAWFDLVGLSPNAKEDEAGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   90 KESAAQVEALIEAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDTNRETPIMMAH 169
Cdd:pfam02230  84 KNSAETIEELIDAEQKKGIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPTKFPSHPNLVTKKTPIFLIH 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504790830  170 GEQDEVVPVFMGNAAFKTLSESGFNATWQTYT-MQHNVCMQELNDISAWLQKVL 222
Cdd:pfam02230 164 GEEDPVVPLALGKLAKEYLKTSLNKVELKIYEgLAHSICGREMQDIKKFLSKHI 217
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
6-220 5.59e-17

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 76.19  E-value: 5.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   6 LPCVEINPSTTPDACVIWLHGLGDSGHGFAPIVPELkLPESMAVkflfpHAPERPvtinG-GMRMRAwydiksldfesRA 84
Cdd:COG2267   16 LRGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEAL-AAAGYAV-----LAFDLR----GhGRSDGP-----------RG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  85 DLEGVKESAAQVEALIEAQIESgiPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGSEA-------- 156
Cdd:COG2267   75 HVDSFDDYVDDLRAALDALRAR--PGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSArwlralrl 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504790830 157 -KDTNR-ETPIMMAHGEQDEVVPVFMGNAAFKTLSEsgfNATWQTYT-MQHNVCMQE-----LNDISAWLQK 220
Cdd:COG2267  153 aEALARiDVPVLVLHGGADRVVPPEAARRLAARLSP---DVELVLLPgARHELLNEPareevLAAILAWLER 221
COG4099 COG4099
Predicted peptidase [General function prediction only];
21-200 2.03e-14

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 69.61  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  21 VIWLHGLGDSG--------HGFAPIV-PELKLPESMAVkfLFPHAPERpvtinggmrmRAWYDIKSLDfesradlegvke 91
Cdd:COG4099   52 VLFLHGAGERGtdnekqltHGAPKFInPENQAKFPAIV--LAPQCPED----------DYWSDTKALD------------ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  92 saaQVEALIE-AQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTyMCEPSLLGSEAKdtnreTPIMMAHG 170
Cdd:COG4099  108 ---AVLALLDdLIAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG-GGDPANAANLKK-----VPVWIFHG 178
                        170       180       190
                 ....*....|....*....|....*....|
gi 504790830 171 EQDEVVPVFMGNAAFKTLSESGFNATWQTY 200
Cdd:COG4099  179 AKDDVVPVEESRAMVEALKAAGADVKYTEY 208
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
88-223 1.11e-12

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 65.04  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  88 GVKESAAQVEALIEAQIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALS-----------TYMCEPSLLGSEA 156
Cdd:COG1506   70 GGDEVDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAgvsdlrsyygtTREYTERLMGGPW 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830 157 KDTNR-------------ETPIMMAHGEQDEVVPVFMGNAAFKTLSESGFNATWQTY-----TMQHNVCMQELNDISAWL 218
Cdd:COG1506  150 EDPEAyaarsplayadklKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYpgeghGFSGAGAPDYLERILDFL 229

                 ....*
gi 504790830 219 QKVLG 223
Cdd:COG1506  230 DRHLK 234
PRK11460 PRK11460
putative hydrolase; Provisional
12-196 2.93e-11

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 60.82  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  12 NPSTTPDACVIWLHGLGDSGHGFAPIVPELK--LPESMAVKflfPHAPErPVTINGGmrmRAWYDIKSLDFESRAdlegv 89
Cdd:PRK11460  10 SPDKPAQQLLLLFHGVGDNPVAMGEIGSWFApaFPDALVVS---VGGPE-PSGNGAG---RQWFSVQGITEDNRQ----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  90 KESAAQVEALIE----AQIESGIPSERIVLAGFSQGGVIALHlAPRYANKFAG-VIALS-TYMCEPsllgsEAKDTNreT 163
Cdd:PRK11460  78 ARVAAIMPTFIEtvryWQQQSGVGASATALIGFSQGAIMALE-AVKAEPGLAGrVIAFSgRYASLP-----ETAPTA--T 149
                        170       180       190
                 ....*....|....*....|....*....|...
gi 504790830 164 PIMMAHGEQDEVVPVFMGNAAFKTLSESGFNAT 196
Cdd:PRK11460 150 TIHLIHGGEDPVIDVAHAVAAQEALISLGGDVT 182
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
21-200 5.20e-10

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: 57.32  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  21 VIWLHGLGDSGHGFAPIVPELklpesmavkflfphAPERPVTInggmrmrawYDI----KSLDFESRADLEGVkesAAQV 96
Cdd:COG0596   26 VVLLHGLPGSSYEWRPLIPAL--------------AAGYRVIA---------PDLrghgRSDKPAGGYTLDDL---ADDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  97 EALIEAQiesGIpsERIVLAGFSQGGVIALHLAPRYANKFAGVIALS-------TYMCEP--------SLLGSEAKDTNR 161
Cdd:COG0596   80 AALLDAL---GL--ERVVLVGHSMGGMVALELAARHPERVAGLVLVDevlaalaEPLRRPglapealaALLRALARTDLR 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504790830 162 E------TPIMMAHGEQDEVVPVFMGNAAFKTLSesgfNATWQTY 200
Cdd:COG0596  155 ErlaritVPTLVIWGEKDPIVPPALARRLAELLP----NAELVVL 195
LpqC COG3509
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ...
21-186 1.62e-09

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


Pssm-ID: 442732 [Multi-domain]  Cd Length: 284  Bit Score: 56.55  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  21 VIWLHGLGDSGHGFA------PIVPElklpESMAVkfLFPHAPerpvtinGGMRMRAWYDiksldFESRADLEGVKESAA 94
Cdd:COG3509   56 VVALHGCGGSAADFAagtglnALADR----EGFIV--VYPEGT-------GRAPGRCWNW-----FDGRDQRRGRDDVAF 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  95 qVEALIEaQIES--GIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSllGSEAKDTNRETPIMMAHGEQ 172
Cdd:COG3509  118 -IAALVD-DLAAryGIDPKRVYVTGLSAGGAMAYRLACEYPDVFAAVAPVAGLPYGAA--SDAACAPGRPVPVLVIHGTA 193
                        170
                 ....*....|....
gi 504790830 173 DEVVPVFMGNAAFK 186
Cdd:COG3509  194 DPTVPYAGAEETLA 207
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
93-200 1.03e-08

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 53.43  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  93 AAQVEALIE-AQIESGIPSERIVLAGFSQGGVIALHLAPRYAnKFAGVIALStymcePSLLGSEAKDTNRE--TPIMMAH 169
Cdd:COG0412   90 AADLRAALDwLKAQPEVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAVSFY-----GGLPADDLLDLAARikAPVLLLY 163
                         90       100       110
                 ....*....|....*....|....*....|.
gi 504790830 170 GEQDEVVPVFMGNAAFKTLSESGFNATWQTY 200
Cdd:COG0412  164 GEKDPLVPPEQVAALEAALAAAGVDVELHVY 194
Fes COG2382
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
111-200 2.77e-08

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


Pssm-ID: 441948 [Multi-domain]  Cd Length: 314  Bit Score: 52.93  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830 111 ERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYMCEPSLLGS--------EAKDTNRETPIMMAHGEQDEVVPvfmGN 182
Cdd:COG2382  196 EHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSFWWPPGDADrggwaellAAGAPKKPLRFYLDVGTEDDLLE---AN 272
                         90
                 ....*....|....*....
gi 504790830 183 AAF-KTLSESGFNATWQTY 200
Cdd:COG2382  273 RALaAALKAKGYDVEYREF 291
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
107-190 6.35e-08

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 51.45  E-value: 6.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830 107 GIPSERIVLAGFSQGGVIALHLAPRYaNKFAGVIALSTYMCEPSLLGSEAKDTNRE------------------------ 162
Cdd:COG1073  105 GVDPERIGLLGISLGGGYALNAAATD-PRVKAVILDSPFTSLEDLAAQRAKEARGAylpgvpylpnvrlasllndefdpl 183
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504790830 163 -------TPIMMAHGEQDEVVPVFMGNAAFKTLSE 190
Cdd:COG1073  184 akiekisRPLLFIHGEKDEAVPFYMSEDLYEAAAE 218
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
65-223 9.45e-07

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 47.61  E-value: 9.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   65 GGMRMRAWYDI-----KSLDFEsraDLEGVkesaaqVEALIEaqiESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGV 139
Cdd:pfam00326  25 SGGYGEAFHDAgkgdlGQNEFD---DFIAA------AEYLIE---QGYTDPDRLAIWGGSYGGYLTGAALNQRPDLFKAA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  140 IA------LSTYMCEPSL------LGSEAKDTNRE-----------------TPIMMAHGEQDEVVPVFMGNAAFKTLSE 190
Cdd:pfam00326  93 VAhvpvvdWLAYMSDTSLpfteryMEWGNPWDNEEgydylspyspadnvkvyPPLLLIHGLLDDRVPPWQSLKLVAALQR 172
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 504790830  191 SGFNATWQTYT------MQHNVCMQELNDISAWLQKVLG 223
Cdd:pfam00326 173 KGVPFLLLIFPdeghgiGKPRNKVEEYARELAFLLEYLG 211
FSH1 pfam03959
Serine hydrolase (FSH1); This is a family of serine hydrolases.
24-177 3.16e-06

Serine hydrolase (FSH1); This is a family of serine hydrolases.


Pssm-ID: 461110  Cd Length: 208  Bit Score: 46.12  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   24 LHGLGDSGHGFAP----IVPELKlpeSMAVKFLFPHAP---ERPVTINGGMR----------MRAWYDiKSLDFESRADL 86
Cdd:pfam03959   9 LHGFGQSGEIFRAktgaLRKLLK---KLGVEFVYLDAPfelAEPADLPGSESekdegeddepYRAWFF-GDDDTNEYLGL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   87 EgvkESaaqVEALIEAQIESGiPSERIVlaGFSQGGVIA-------LHLAPRYANKFAGVIALSTYMCEPSLLGSEAKDT 159
Cdd:pfam03959  85 D---ES---LDYVRDYIKENG-PFDGIL--GFSQGAALAailasllEEGLPLSHPPLKFAILFSGFRPRPPIYQEYYSED 155
                         170
                  ....*....|....*...
gi 504790830  160 NRETPIMMAHGEQDEVVP 177
Cdd:pfam03959 156 PIQTPSLHVIGELDTVVP 173
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
20-144 8.06e-06

Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 43.28  E-value: 8.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  20 CVIWLHGLGDSGHGFAPIVPELKlpesmavkflfphaperpvtiNGGmrmrawYDIKSLDFESRADleGVKESAAQVEAL 99
Cdd:COG1075    7 PVVLVHGLGGSAASWAPLAPRLR---------------------AAG------YPVYALNYPSTNG--SIEDSAEQLAAF 57
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 504790830 100 IEaQIESGIPSERIVLAGFSQGGVIALHLA--PRYANKFAGVIALST 144
Cdd:COG1075   58 VD-AVLAATGAEKVDLVGHSMGGLVARYYLkrLGGAAKVARVVTLGT 103
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
111-178 5.85e-05

Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 42.62  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830 111 ERIVLAGFSQGGVIALHLAPRYANkFAGVIALST--YMCEPSLL---------------GSEAKDTNRE----------- 162
Cdd:COG1647   84 DKVIVIGLSMGGLLALLLAARYPD-VAGLVLLSPalKIDDPSAPllpllkylarslrgiGSDIEDPEVAeyaydrtplra 162
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504790830 163 -------------------TPIMMAHGEQDEVVPV 178
Cdd:COG1647  163 laelqrlirevrrdlpkitAPTLIIQSRKDEVVPP 197
COG2945 COG2945
Alpha/beta superfamily hydrolase [General function prediction only];
110-177 1.14e-04

Alpha/beta superfamily hydrolase [General function prediction only];


Pssm-ID: 442188 [Multi-domain]  Cd Length: 201  Bit Score: 41.69  E-value: 1.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830 110 SERIVLAGFSQGGVIALHLAPRYAnKFAGVIALST--YMCEPSLLGSEAKDTnretpiMMAHGEQDEVVP 177
Cdd:COG2945   95 PLPLWLAGFSFGAYVALQLAMRLP-EVEGLILVAPpvNRYDFSFLAPCPAPT------LVIHGEQDEVVP 157
Esterase_713_like-1 cd12808
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
93-160 1.21e-04

Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated cyclic compounds; This family contains uncharacterized proteins similar to a novel bacterial esterase (Alcaligenes esterase 713) with the alpha/beta hydrolase fold but does not contain the GXSXXG pentapeptide around the active site serine residue as commonly seen in other enzymes of this class. Esterase 713 shows negligible sequence homology to other esterase and lipase enzymes. It is active as a dimer and cleaves esters on halogenated cyclic compounds though its natural substrate is unknown.


Pssm-ID: 214007  Cd Length: 309  Bit Score: 42.23  E-value: 1.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504790830  93 AAQVEALIeAQIESGIPSeriVLAGFSQGGVIALHLAPRYANKFAGVIALstymcEPSLLGSEAKDTN 160
Cdd:cd12808  174 ALTLAAYD-ALLDRVGPC---IVVAHSQGGGFAFEAARARPDLVRAVVAL-----EPSGAPDPAEAAP 232
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
21-146 1.59e-04

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 41.34  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   21 VIWLHGLGDSGHGFAPIVPELklpeSMAVKFLFphAPERPvtiNGGmrmrawydiKSlDFESRADLEGVKESAAQVEALI 100
Cdd:pfam00561   3 VLLLHGLPGSSDLWRKLAPAL----ARDGFRVI--ALDLR---GFG---------KS-SRPKAQDDYRTDDLAEDLEYIL 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 504790830  101 EAqiesgIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTYM 146
Cdd:pfam00561  64 EA-----LGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALD 104
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
17-151 4.83e-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: 39.89  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   17 PDACVIWLHGLGDSGHGFAPIVPELKLPeSMAVkFLFPH------APERpvtinggmrmrawYDIKSLDfESRADLegvk 90
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQ-GFAV-YAYDHrghgrsDGKR-------------GHVPSFD-DYVDDL---- 62
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504790830   91 esAAQVEALIEAQiesgiPSERIVLAGFSQGGVIALHLAPRYANKFAGVIaLSTYMCEPSL 151
Cdd:pfam12146  63 --DTFVDKIREEH-----PGLPLFLLGHSMGGLIAALYALRYPDKVDGLI-LSAPALKIKP 115
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
87-223 6.16e-04

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 39.47  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830  87 EGVKESAAQVEALIEAQIESGIPSERIVLAGFSQGG----VIALHLAPRYANKFAGVIALS-TYMCEPSLLGSEAKDTnr 161
Cdd:COG0657   62 AALEDAYAALRWLRANAAELGIDPDRIAVAGDSAGGhlaaALALRARDRGGPRPAAQVLIYpVLDLTASPLRADLAGL-- 139
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504790830 162 eTPIMMAHGEQDEVVPvfmGNAAF-KTLSESGFNATWQTY-TMQHNVCM--------QELNDISAWLQKVLG 223
Cdd:COG0657  140 -PPTLIVTGEADPLVD---ESEALaAALRAAGVPVELHVYpGGGHGFGLlaglpearAALAEIAAFLRRALA 207
Esterase pfam00756
Putative esterase; This family contains Esterase D. However it is not clear if all members of ...
114-145 8.73e-04

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: 39.37  E-value: 8.73e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 504790830  114 VLAGFSQGGVIALHLAPRYANKFAGVIALSTY 145
Cdd:pfam00756 113 ALAGQSMGGLGALYLALKYPDLFGSVSSFSPI 144
Esterase_PHB pfam10503
Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), ...
17-178 3.70e-03

Esterase PHB depolymerase; This family of proteins include acetyl xylan esterases (AXE), feruloyl esterases (FAE), and poly(3-hydroxybutyrate) (PHB) depolymerases.


Pssm-ID: 431322 [Multi-domain]  Cd Length: 222  Bit Score: 37.35  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   17 PDACVIWLHGLGDSGHGFAPIVPELKLPESMAVKFLFPHAPERpvtiNGGMRMRAWYDiksldfESRADLEGvkESAAQV 96
Cdd:pfam10503  17 PMPLVVMLHGCKQHADDFAAGTRINALADELGFAVLYPEQSKH----AHAHKCWNWFD------EQGAARGG--GEAASI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   97 EALIEAQIESG-IPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALS--TYMCEPSLLGS----------------EAK 157
Cdd:pfam10503  85 AALAKAIAAAHrLDGARVYLAGLSAGAALAALLAHCYPDVFAAVGLHSglPFGCAADAASAldamrrgpgpapgaliDAA 164
                         170       180
                  ....*....|....*....|....
gi 504790830  158 DTNRETPIMMA---HGEQDEVVPV 178
Cdd:pfam10503 165 SDVRSYPALPAiifHGDADSTVAS 188
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
87-172 4.71e-03

2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 37.91  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504790830   87 EGVKESAAQVEALIEA--QIESGIPSERIVLAGFSQGGVIALHLAPRYANKFAGVIALSTymcEPSLLGSE------AKD 158
Cdd:PLN02980 1419 ETQTEPTLSVELVADLlyKLIEHITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISG---SPGLKDEVarkirsAKD 1495
                          90
                  ....*....|....
gi 504790830  159 TNReTPIMMAHGEQ 172
Cdd:PLN02980 1496 DSR-ARMLIDHGLE 1508
 
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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