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Conserved domains on  [gi|654546311|ref|WP_028014017|]
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MULTISPECIES: esterase [Enterobacter]

Protein Classification

hydrolase( domain architecture ID 10013806)

uncharacterized hydrolase similar to Escherichia coli esterase YpfH

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11460 PRK11460
putative hydrolase; Provisional
1-231 1.32e-154

putative hydrolase; Provisional


:

Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 428.30  E-value: 1.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   1 MKHDHFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSIGGVEPCG-PDGRQWFPVQGVTEENRQARI 79
Cdd:PRK11460   1 MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGSWFAPAFPDALVVSVGGPEPSGnGAGRQWFSVQGITEDNRQARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  80 DAIMPTFIDIVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATLPTSATTQTTIHLIHGGEDR 159
Cdd:PRK11460  81 AAIMPTFIETVRYWQQQSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGRYASLPETAPTATTIHLIHGGEDP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546311 160 VIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHLRYTVPKHYFDEALSGGKPNDDDIVEFM 231
Cdd:PRK11460 161 VIDVAHAVAAQEALISLGGDVTLDIVEDLGHAIDPRLMQFALDRLRYTVPKRYWDEALSGGKPGDDDVIEMM 232
 
Name Accession Description Interval E-value
PRK11460 PRK11460
putative hydrolase; Provisional
1-231 1.32e-154

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 428.30  E-value: 1.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   1 MKHDHFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSIGGVEPCG-PDGRQWFPVQGVTEENRQARI 79
Cdd:PRK11460   1 MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGSWFAPAFPDALVVSVGGPEPSGnGAGRQWFSVQGITEDNRQARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  80 DAIMPTFIDIVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATLPTSATTQTTIHLIHGGEDR 159
Cdd:PRK11460  81 AAIMPTFIETVRYWQQQSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGRYASLPETAPTATTIHLIHGGEDP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546311 160 VIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHLRYTVPKHYFDEALSGGKPNDDDIVEFM 231
Cdd:PRK11460 161 VIDVAHAVAAQEALISLGGDVTLDIVEDLGHAIDPRLMQFALDRLRYTVPKRYWDEALSGGKPGDDDVIEMM 232
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
3-207 3.04e-62

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: 193.75  E-value: 3.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311    3 HDHFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSIGGVEPCG-PDGR---QWFPVQGVTEENRQ-- 76
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKTEAPLPNIKFIFPHGPEIPVTlNGGMrmpAWFDLVGLSPNAKEde 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   77 ARIDAIMPTFIDIVRYWQQQsGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATL------PTSATTQTTI 150
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKK-GIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPtkfpshPNLVTKKTPI 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 654546311  151 HLIHGGEDRVIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHLRYT 207
Cdd:pfam02230 160 FLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIKKFLSKH 216
YpfH COG0400
Predicted esterase [General function prediction only];
12-209 4.24e-45

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 149.29  E-value: 4.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  12 DKPAKQLLLLFHGVGDNAVNMGQIGRWFAPvfPEALIVSIGGVEPCGPDGRQWFPVQGVTEENRQARIDAIMPTFIDIVR 91
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAL--PGAAVLAPRAPVPEGPGGRAWFDLSFLEGREDEEGLAAAAEALAAFID 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  92 YWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYAT-----LPTSATTQTTIHLIHGGEDRVIELSHA 166
Cdd:COG0400   79 ELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGeealpAPEAALAGTPVFLAHGTQDPVIPVERA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 654546311 167 VAAQEALVREGGDVTLDIVdDLGHAIDDRSMQFALDHLRYTVP 209
Cdd:COG0400  159 REAAEALEAAGADVTYREY-PGGHEISPEELADARAWLAERLA 200
 
Name Accession Description Interval E-value
PRK11460 PRK11460
putative hydrolase; Provisional
1-231 1.32e-154

putative hydrolase; Provisional


Pssm-ID: 183144 [Multi-domain]  Cd Length: 232  Bit Score: 428.30  E-value: 1.32e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   1 MKHDHFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSIGGVEPCG-PDGRQWFPVQGVTEENRQARI 79
Cdd:PRK11460   1 MKHDHFVVQSPDKPAQQLLLLFHGVGDNPVAMGEIGSWFAPAFPDALVVSVGGPEPSGnGAGRQWFSVQGITEDNRQARV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  80 DAIMPTFIDIVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATLPTSATTQTTIHLIHGGEDR 159
Cdd:PRK11460  81 AAIMPTFIETVRYWQQQSGVGASATALIGFSQGAIMALEAVKAEPGLAGRVIAFSGRYASLPETAPTATTIHLIHGGEDP 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546311 160 VIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHLRYTVPKHYFDEALSGGKPNDDDIVEFM 231
Cdd:PRK11460 161 VIDVAHAVAAQEALISLGGDVTLDIVEDLGHAIDPRLMQFALDRLRYTVPKRYWDEALSGGKPGDDDVIEMM 232
Abhydrolase_2 pfam02230
Phospholipase/Carboxylesterase; This family consists of both phospholipases and ...
3-207 3.04e-62

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: 193.75  E-value: 3.04e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311    3 HDHFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSIGGVEPCG-PDGR---QWFPVQGVTEENRQ-- 76
Cdd:pfam02230   1 NGCAEVVSPRDPAQATVIFLHGLGDSGHGWADAAKTEAPLPNIKFIFPHGPEIPVTlNGGMrmpAWFDLVGLSPNAKEde 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   77 ARIDAIMPTFIDIVRYWQQQsGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATL------PTSATTQTTI 150
Cdd:pfam02230  81 AGIKNSAETIEELIDAEQKK-GIPSSRIIIGGFSQGAMLALYSALTLPLPLGGIVAFSGFLPLPtkfpshPNLVTKKTPI 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 654546311  151 HLIHGGEDRVIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHLRYT 207
Cdd:pfam02230 160 FLIHGEEDPVVPLALGKLAKEYLKTSLNKVELKIYEGLAHSICGREMQDIKKFLSKH 216
YpfH COG0400
Predicted esterase [General function prediction only];
12-209 4.24e-45

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 149.29  E-value: 4.24e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  12 DKPAKQLLLLFHGVGDNAVNMGQIGRWFAPvfPEALIVSIGGVEPCGPDGRQWFPVQGVTEENRQARIDAIMPTFIDIVR 91
Cdd:COG0400    1 GGPAAPLVVLLHGYGGDEEDLLPLAPELAL--PGAAVLAPRAPVPEGPGGRAWFDLSFLEGREDEEGLAAAAEALAAFID 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  92 YWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYAT-----LPTSATTQTTIHLIHGGEDRVIELSHA 166
Cdd:COG0400   79 ELEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGeealpAPEAALAGTPVFLAHGTQDPVIPVERA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 654546311 167 VAAQEALVREGGDVTLDIVdDLGHAIDDRSMQFALDHLRYTVP 209
Cdd:COG0400  159 REAAEALEAAGADVTYREY-PGGHEISPEELADARAWLAERLA 200
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
52-191 2.34e-09

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


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 55.74  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  52 GGVEPCGPDGRQWFPVQGVTEENRQARIDAImptfidiVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASrVI 131
Cdd:COG0412   66 GRGGPGDDPDEARALMGALDPELLAADLRAA-------LDWLKAQPEVDAGRVGVVGFCFGGGLALLAAARGPDLAA-AV 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546311 132 AFNGRYATLPTSATTQTT---IHLIHGGEDRVIELSHAVAAQEALVREGGDVTLDIVDDLGHA 191
Cdd:COG0412  138 SFYGGLPADDLLDLAARIkapVLLLYGEKDPLVPPEQVAALEAALAAAGVDVELHVYPGAGHG 200
DLH pfam01738
Dienelactone hydrolase family;
7-191 9.88e-08

Dienelactone hydrolase family;


Pssm-ID: 396343 [Multi-domain]  Cd Length: 213  Bit Score: 50.81  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311    7 VVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFAPVFPEALIVSI--GGVEPCGPDGRQwfpvQGVTEENRQARIDAIMP 84
Cdd:pfam01738   3 YLATPKNPPWPVVVVFQEIFGVNDNIREIADRLADEGYVALAPDLyfRQGDPNDEADAA----RAMFELVSKRVMEKVLD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   85 TFIDIVRYWQQQSGVGADATALIGFSQGSIMSLEsVKAQPGLASRVIAFNGRYATLPTSATT--QTTIHLIHGGEDRVIE 162
Cdd:pfam01738  79 DLEAAVNYLKSQPEVSPKKVGVVGYCMGGALAVL-LAAKGPLVDAAVGFYGVGPEPPLIEAPdiKAPILFHFGEEDHFVP 157
                         170       180
                  ....*....|....*....|....*....
gi 654546311  163 LSHAVAAQEALVREGGDVTLDIVDDLGHA 191
Cdd:pfam01738 158 ADSRELIEEALKAANVDHQIHSYPGAGHA 186
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
5-192 1.14e-07

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 50.77  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   5 HFVVQSPDKPAKQLLLLFHGVGDNAVNMGQIGRWFApvfpEAlivsigGVEPCGPDgrqwFPVQGVTEENR--QARIDAI 82
Cdd:COG2267   17 RGRRWRPAGSPRGTVVLVHGLGEHSGRYAELAEALA----AA------GYAVLAFD----LRGHGRSDGPRghVDSFDDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  83 MPTFIDIVRYWQQQSGvgaDATALIGFSQGSIMSLESVKAQPGLASRVIAFNGRYATLPTSATTQTT------------- 149
Cdd:COG2267   83 VDDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPLLGPSARWlralrlaealari 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 654546311 150 ---IHLIHGGEDRVIELSHAVAAQEALvreGGDVTLDIVDDLGHAI 192
Cdd:COG2267  160 dvpVLVLHGGADRVVPPEAARRLAARL---SPDVELVLLPGARHEL 202
COG4099 COG4099
Predicted peptidase [General function prediction only];
5-192 2.92e-06

Predicted peptidase [General function prediction only];


Pssm-ID: 443275 [Multi-domain]  Cd Length: 235  Bit Score: 46.50  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311   5 HFVVQSPD--KPAKQ--LLLLFHGVG----DNAVNMGQ-----IGRWFAPVFPeALIVSiggvePCGPDGRQWfpvqgvt 71
Cdd:COG4099   34 PYRLYLPKgyDPGKKypLVLFLHGAGergtDNEKQLTHgapkfINPENQAKFP-AIVLA-----PQCPEDDYW------- 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  72 eenrqaRIDAIMPTFIDIVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGL--ASRVIAFNGRYATLPTSATTqtT 149
Cdd:COG4099  101 ------SDTKALDAVLALLDDLIAEYRIDPDRIYLTGLSMGGYGTWDLAARYPDLfaAAVPICGGGDPANAANLKKV--P 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 654546311 150 IHLIHGGEDRVIELSHAVAAQEALVREGGDVTLDIVDDLGHAI 192
Cdd:COG4099  173 VWIFHGAKDDVVPVEESRAMVEALKAAGADVKYTEYPGVGHNS 215
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
87-204 1.24e-05

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 45.01  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546311  87 IDIVRYWQQQSGVGADATALIGFSQGSIMSLESVKAQPGLASRVIAFNG----------------RYATLPTSAT----T 146
Cdd:COG1506   78 LAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGvsdlrsyygttreyteRLMGGPWEDPeayaA 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546311 147 QTTIH----------LIHGGEDRVIELSHAVAAQEALVREGGDVTLDIVDDLGHAIDDRSMQFALDHL 204
Cdd:COG1506  158 RSPLAyadklktpllLIHGEADDRVPPEQAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLERI 225
 
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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