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Conserved domains on  [gi|16128662|ref|NP_415212|]
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esterase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

esterase( domain architecture ID 11484866)

esterase similar esterase YbfF, which belongs to alpha/beta hydrolase family and cleaves an ester bond utilizing a water molecule; may have broad substrate specificity for long-chain substrates as well as substrates of small molecular weight

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


:

Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 532.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 16128662  241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 532.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 16128662  241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-253 9.45e-40

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: 137.05  E-value: 9.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596  25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  97 ALTALASDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128662 177 vlwdqyphivgWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLN 253
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-241 2.84e-22

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: 91.80  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    94 AVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 16128662   238 AEKP 241
Cdd:pfam00561 242 LEGP 245
 
Name Accession Description Interval E-value
PRK10673 PRK10673
esterase;
1-254 0e+00

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 532.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673   1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673  81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                        250
                 ....*....|....
gi 16128662  241 PDAVLRAIRRYLND 254
Cdd:PRK10673 241 PDAVLRAIRRYLND 254
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 18-253 9.45e-40

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: 137.05  E-value: 9.45e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596  25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  97 ALTALASDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596 105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128662 177 vlwdqyphivgWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLRAIRRYLN 253
Cdd:COG0596 154 -----------RERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLA 219
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 18-241 2.84e-22

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: 91.80  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    94 AVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 16128662   238 AEKP 241
Cdd:pfam00561 242 LEGP 245
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 18-252 8.67e-15

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 73.05  E-value: 8.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   18 PIVLVHGLFGSLDN-LGVLArDLVNDHNIIQVDMRNHGLS-PRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAV 95
Cdd:PRK14875 133 PVVLIHGFGGDLNNwLFNHA-ALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   96 MALTALASDRIDKLVAidIAP--------VDYhvrrhdeIFAAINAVSESDAQ-------------TRQQAAAIMRQhLN 154
Cdd:PRK14875 212 LRLAARAPQRVASLTL--IAPaglgpeinGDY-------IDGFVAAESRRELKpvlellfadpalvTRQMVEDLLKY-KR 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  155 EEGVIQFLLK----SFVDGEWRFNV-PVLWD-QYPHIVGW---EKIPAWDHpALFIPGGnspyvseqyrddllaqfpqAR 225
Cdd:PRK14875 282 LDGVDDALRAladaLFAGGRQRVDLrDRLASlAIPVLVIWgeqDRIIPAAH-AQGLPDG-------------------VA 341

                        250       260
                 ....*....|....*....|....*..
gi 16128662  226 AHVIAGAGHWVHAEKPDAVLRAIRRYL 252
Cdd:PRK14875 342 VHVLPGAGHMPQMEAAADVNRLLAEFL 368
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
18-254 2.07e-13

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 67.33  E-value: 2.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  18 PIVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP--VMNYPAMAQDL---VDTLDAQQIDKATFIGHSMG 91
Cdd:COG2267  30 TVVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDGPRghVDSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  92 GKAVMALTALASDRIDKLVAidIAPVDYHvrrhdeifaainavsesdaqtrqqaaaimrqhlneegviqfllksfvDGEW 171
Cdd:COG2267 110 GLIALLYAARYPDRVAGLVL--LAPAYRA-----------------------------------------------DPLL 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662 172 RFNVPVLWDQYPhivgWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQF-PQARAHVIAGAGHWVHAEKP-DAVLRAIR 249
Cdd:COG2267 141 GPSARWLRALRL----AEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNEPArEEVLAAIL 216


                ....*
gi 16128662 250 RYLND 254
Cdd:COG2267 217 AWLER 221
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 19-247 3.48e-13

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 66.73  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    19 IVLVHGLFGSLDNLGVLARDLVNDHNiiqVDMRNHGLSPRDPVmNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVMAL 98
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAAGVAVLA---PDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    99 TALAsdridKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVPVL 178
Cdd:pfam12697  77 AAAA-----LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16128662   179 WDQYPHivgWEKIPAWdhpaLFIPGGNSPYVSEQYRdDLLAQFPQARAHVIAGAGHWVHaEKPDAVLRA 247
Cdd:pfam12697 152 LLPLAA---WRDLPVP----VLVLAEEDRLVPELAQ-RLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
PGAP1 pfam07819
PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an ...
 18-134 2.02e-07

PGAP1-like protein; The sequences found in this family are similar to PGAP1. This is an endoplasmic reticulum membrane protein with a catalytic serine containing motif that is conserved in a number of lipases. PGAP1 functions as a GPI inositol-deacylase; this deacylation is important for the efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi body. This entry also includes Tgl2, a mitochondria protein that serves as a triacylglycerol lipase in budding yeasts.


Pssm-ID: 369540  Cd Length: 233  Bit Score: 50.44  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPV---MNYPAMAQD---LVDTLD--------AQQIDKA 83
Cdd:pfam07819   6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGFHLDFFsvdFNEELSAFHgrtLLDQAEylndairyILSLYAS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128662    84 TF--------IGHSMGGK---AVMALTALASDRIDKLVAIDiAPVDYHVRRHD----EIFAAINAV 134
Cdd:pfam07819  86 GRpgptsvilIGHSMGGIvarAALTLPNYIPQSVNTIITLS-SPHAKPPLTFDgdilKFYERLNAF 150
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 18-112 4.26e-07

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 47.13  E-value: 4.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  18 PIVLVHGLFGSLDNLGVLARDLvndhniiqvdmRNHGLSPRdpVMNYPAMAQDLVDTLD--AQQID---------KATFI 86
Cdd:COG1075   7 PVVLVHGLGGSAASWAPLAPRL-----------RAAGYPVY--ALNYPSTNGSIEDSAEqlAAFVDavlaatgaeKVDLV 73

                        90       100       110
                ....*....|....*....|....*....|
gi 16128662  87 GHSMGGkaVMALTALAS----DRIDKLVAI 112
Cdd:COG1075  74 GHSMGG--LVARYYLKRlggaAKVARVVTL 101
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
19-253 1.10e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.09  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  19 IVLVHGLFGSLDN-LGVLARDLVND-HNIIQVDMRNHGLSPRDPvmnYPAMAQDLVDTLDA----QQIDKATF--IGHSM 90
Cdd:COG1506  26 VVYVHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAGDW---GGDEVDDVLAAIDYlaarPYVDPDRIgiYGHSY 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  91 GGKAVMALTALASDRIDklVAIDIAPVdyhvrrhdeifaainavseSDAQTRQQAAAIMRQHLNeegviqfllksfvdGE 170
Cdd:COG1506 103 GGYMALLAAARHPDRFK--AAVALAGV-------------------SDLRSYYGTTREYTERLM--------------GG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662 171 WRFNVPVLWDQYPHivgwEKIPAWDHPALFIPGGNSPYV----SEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
Cdd:COG1506 148 PWEDPEAYAARSPL----AYADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLE 223


                ....*..
gi 16128662 247 AIRRYLN 253
Cdd:COG1506 224 RILDFLD 230
COG4814 COG4814
Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];
1-112 8.66e-06

Uncharacterized conserved protein with an alpha/beta hydrolase fold [Function unknown];


Pssm-ID: 443842  Cd Length: 286  Bit Score: 45.70  E-value: 8.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLV----------------------------NDHN-IIQVDMR 51
Cdd:COG4814  28 TKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNekygvghkvltvtvskdgkitysgkirkNAKNpIIQVGFE 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128662  52 NHglspRDPVMNYPAMAQDLVDTLDAQ-QIDKATFIGHSMGGKAVMA-LTALASDR----IDKLVAI 112
Cdd:COG4814 108 DN----RDSIKKQAKWLKKVLKYLKKKyGFKKFNAVGHSMGGLALTYyLEKYGNDKslpkLNKLVTI 170
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
19-253 1.19e-05

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 45.32  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDPV-MNYPAMAQDLVDTLD--AQQIDKATFIGHSMGGka 94
Cdd:COG1647  18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEilKAGYDKVIVIGLSMGG-- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  95 VMALtALASDR--IDKLVAIDiAPVDY--------HVRRHdeIFAAINAVSESDAQTRQQAAAIMRQHLNeeGVIQFLLk 164
Cdd:COG1647  96 LLAL-LLAARYpdVAGLVLLS-PALKIddpsapllPLLKY--LARSLRGIGSDIEDPEVAEYAYDRTPLR--ALAELQR- 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662 165 sfvdgewrfnvpvLWDQYPhivgwEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIA--GAGHWVHAEK-P 241
Cdd:COG1647 169 -------------LIREVR-----RDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWleDSGHVITLDKdR 230

                       250
                ....*....|..
gi 16128662 242 DAVLRAIRRYLN 253
Cdd:COG1647 231 EEVAEEILDFLE 242
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 4-123 1.65e-05

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 45.11  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    4 NIRAQTAQNQhnNSPIVLVHGLFGSLD----NLGVLARDlvndHNIIQVDMRNHGLS--------PRDPVMNYPAMAQDL 71
Cdd:PLN02824  19 NIRYQRAGTS--GPALVLVHGFGGNADhwrkNTPVLAKS----HRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQL 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 16128662   72 VDTLDAQQIDKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRR 123
Cdd:PLN02824  93 NDFCSDVVGDPAFVICNSVGGVVGLQAAVDAPELVRGVMLINISLRGLHIKK 144
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 19-252 2.97e-05

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 44.14  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP-VMNYPAM--AQDLVDTL------DAQQIdkaTFIGH 88
Cdd:COG1073  40 VVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESEGEPrEEGSPERrdARAAVDYLrtlpgvDPERI---GLLGI 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662  89 SMGGkaVMALTALASDRIDKLVAIDIAPVDYhvrrhdeifaainavsesDAQTRQQAAAIMRQHLneeGVIQFL----LK 164
Cdd:COG1073 117 SLGG--GYALNAAATDPRVKAVILDSPFTSL------------------EDLAAQRAKEARGAYL---PGVPYLpnvrLA 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662 165 SFVDGEWRfnvPVlwdqyphivgwEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARA-HVIAGAGH----WVHAE 239
Cdd:COG1073 174 SLLNDEFD---PL-----------AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvdlyDRPEE 239

                       250
                ....*....|....
gi 16128662 240 KPDAVLRA-IRRYL 252
Cdd:COG1073 240 EYFDKLAEfFKKNL 253
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 19-116 4.70e-05

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: 43.36  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662    19 IVLVHGLFGSLDNLGVLARDLVndHNIIQV---DMRNHGLSP--RDPVMNYPAMAQDL---VDTLDAQQIDKATFI-GHS 89
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALA--AQGFAVyayDHRGHGRSDgkRGHVPSFDDYVDDLdtfVDKIREEHPGLPLFLlGHS 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 16128662    90 MGGKAVMALTALASDRIDKLV----AIDIAP 116
Cdd:pfam12146  85 MGGLIAALYALRYPDKVDGLIlsapALKIKP 115
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 19-104 2.13e-03

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 38.28  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128662   19 IVLVHGLFGSLDN-LGVLarDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM- 96
Cdd:PRK11126   5 LVFLHGLLGSGQDwQPVG--EALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMy 82


                 ....*....
gi 16128662   97 -ALTALASD 104
Cdd:PRK11126  83 yACQGLAGG 91
 
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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