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Conserved domains on  [gi|1487551986|gb|AYG20196|]
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alpha/beta hydrolase [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 1487551986   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673    1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673   81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                         250
                  ....*....|....
gi 1487551986 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 1487551986   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673    1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673   81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                         250
                  ....*....|....
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  97 ALTALASDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596   105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  94 AVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 1487551986 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 1487551986   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQI 80
Cdd:PRK10673    1 MKLNIRAQTAQNPHNNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  81 DKATFIGHSMGGKAVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQ 160
Cdd:PRK10673   81 EKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAPVDYHVRRHDEIFAAINAVSEAGATTRQQAAAIMRQHLNEEGVIQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVHAEK 240
Cdd:PRK10673  161 FLLKSFVDGEWRFNVPVLWDQYPHIVGWEKIPAWPHPALFIRGGNSPYVTEAYRDDLLAQFPQARAHVIAGAGHWVHAEK 240

                         250
                  ....*....|....
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPR-DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM 96
Cdd:COG0596    25 PVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKpAGGYTLDDLADDLAALLDALGLERVVLVGHSMGGMVAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  97 ALTALASDRIDKLVAIDiapvdyhvrrhdeifaainavsesdaqtrqQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVp 176
Cdd:COG0596   105 ELAARHPERVAGLVLVD------------------------------EVLAALAEPLRRPGLAPEALAALLRALARTDL- 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDL-VNDHNIIQVDMRNHGLSPR---DPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGK 93
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSRpkaQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  94 AVMALTALASDRIDKLVAIDIAPVDYHVRRHDEIFAAI-----NAVSESDAQTRQ-QAAAIMRQHLNEEGVIQFLLKSFV 167
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALfpgffDGFVADFAPNPLgRLVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 168 DGEWRFNVPV----------LWDQYPHIVGWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIAGAGHWVH 237
Cdd:pfam00561 162 KRFPSGDYALakslvtgallFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAF 241


                  ....
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDN-LGVLArDLVNDHNIIQVDMRNHGLS-PRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAV 95
Cdd:PRK14875  133 PVVLIHGFGGDLNNwLFNHA-ALAAGRPVIALDLPGHGASsKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  96 MALTALASDRIDKLVAidIAP--------VDYhvrrhdeIFAAINAVSESDAQ-------------TRQQAAAIMRQhLN 154
Cdd:PRK14875  212 LRLAARAPQRVASLTL--IAPaglgpeinGDY-------IDGFVAAESRRELKpvlellfadpalvTRQMVEDLLKY-KR 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 155 EEGVIQFLLK----SFVDGEWRFNV-PVLWD-QYPHIVGW---EKIPAWDHpALFIPGGnspyvseqyrddllaqfpqAR 225
Cdd:PRK14875  282 LDGVDDALRAladaLFAGGRQRVDLrDRLASlAIPVLVIWgeqDRIIPAAH-AQGLPDG-------------------VA 341

                         250       260
                  ....*....|....*....|....*..
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP--VMNYPAMAQDL---VDTLDAQQIDKATFIGHSMG 91
Cdd:COG2267    30 TVVLVHGLGEHSGRYAELAEALAaAGYAVLAFDLRGHGRSDGPRghVDSFDDYVDDLraaLDALRARPGLPVVLLGHSMG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  92 GKAVMALTALASDRIDKLVAidIAPVDYHvrrhdeifaainavsesdaqtrqqaaaimrqhlneegviqfllksfvDGEW 171
Cdd:COG2267   110 GLIALLYAARYPDRVAGLVL--LAPAYRA-----------------------------------------------DPLL 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 172 RFNVPVLWDQYPhivgWEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQF-PQARAHVIAGAGHWVHAEKP-DAVLRAIR 249
Cdd:COG2267   141 GPSARWLRALRL----AEALARIDVPVLVLHGGADRVVPPEAARRLAARLsPDVELVLLPGARHELLNEPArEEVLAAIL 216


                  ....*
gi 1487551986 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 1487551986  19 IVLVHGLFGSLDNLGVLARDLVNDHNiiqVDMRNHGLSPRDPVmNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVMAL 98
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALLAAGVAVLA---PDLPGHGSSSPPPL-DLADLADLAALLDELGAARPVVLVGHSLGGAVALAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  99 TALAsdridKLVAIDIAPVDYHVRRHDEIFAAINAVSESDAQTRQQAAAIMRQHLNEEGVIQFLLKSFVDGEWRFNVPVL 178
Cdd:pfam12697  77 AAAA-----LVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1487551986 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 1487551986  18 PIVLVHGLFGSLDNLGVLARDLVNDHNIIQVDMRNHGLSPRDPV---MNYPAMAQD---LVDTLD--------AQQIDKA 83
Cdd:pfam07819   6 PVLFIPGNAGSYKQVRSIASVAANLYQVLRKLLQNDNGFHLDFFsvdFNEELSAFHgrtLLDQAEylndairyILSLYAS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1487551986  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 1487551986  18 PIVLVHGLFGSLDNLGVLARDLvndhniiqvdmRNHGLSPRdpVMNYPAMAQDLVDTLD--AQQID---------KATFI 86
Cdd:COG1075     7 PVVLVHGLGGSAASWAPLAPRL-----------RAAGYPVY--ALNYPSTNGSIEDSAEqlAAFVDavlaatgaeKVDLV 73

                          90       100       110
                  ....*....|....*....|....*....|
gi 1487551986  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 1487551986  19 IVLVHGLFGSLDN-LGVLARDLVND-HNIIQVDMRNHGLSPRDPvmnYPAMAQDLVDTLDA----QQIDKATF--IGHSM 90
Cdd:COG1506    26 VVYVHGGPGSRDDsFLPLAQALASRgYAVLAPDYRGYGESAGDW---GGDEVDDVLAAIDYlaarPYVDPDRIgiYGHSY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  91 GGKAVMALTALASDRIDklVAIDIAPVdyhvrrhdeifaainavseSDAQTRQQAAAIMRQHLNeegviqfllksfvdGE 170
Cdd:COG1506   103 GGYMALLAAARHPDRFK--AAVALAGV-------------------SDLRSYYGTTREYTERLM--------------GG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 171 WRFNVPVLWDQYPHivgwEKIPAWDHPALFIPGGNSPYV----SEQYRDDLLAQFPQARAHVIAGAGHWVHAEKPDAVLR 246
Cdd:COG1506   148 PWEDPEAYAARSPL----AYADKLKTPLLLIHGEADDRVppeqAERLYEALKKAGKPVELLVYPGEGHGFSGAGAPDYLE 223


                  ....*..
gi 1487551986 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 1487551986   1 MKLNIRAQTAQNQHNNSPIVLVHGLFGSLDNLGVLARDLV----------------------------NDHN-IIQVDMR 51
Cdd:COG4814    28 TKSTVKSLKSKYNSKQTPTIFIHGSGGTANSFNTMINRLNekygvghkvltvtvskdgkitysgkirkNAKNpIIQVGFE 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1487551986  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 1487551986  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDPV-MNYPAMAQDLVDTLD--AQQIDKATFIGHSMGGka 94
Cdd:COG1647    18 VLLLHGFTGSPAEMRPLAEALAkAGYTVYAPRLPGHGTSPEDLLkTTWEDWLEDVEEAYEilKAGYDKVIVIGLSMGG-- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  95 VMALtALASDR--IDKLVAIDiAPVDY--------HVRRHdeIFAAINAVSESDAQTRQQAAAIMRQHLNeeGVIQFLLk 164
Cdd:COG1647    96 LLAL-LLAARYpdVAGLVLLS-PALKIddpsapllPLLKY--LARSLRGIGSDIEDPEVAEYAYDRTPLR--ALAELQR- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 165 sfvdgewrfnvpvLWDQYPhivgwEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARAHVIA--GAGHWVHAEK-P 241
Cdd:COG1647   169 -------------LIREVR-----RDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWleDSGHVITLDKdR 230

                         250
                  ....*....|..
gi 1487551986 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 1487551986   4 NIRAQTAQNQhnNSPIVLVHGLFGSLD----NLGVLARDlvndHNIIQVDMRNHGLS--------PRDPVMNYPAMAQDL 71
Cdd:PLN02824   19 NIRYQRAGTS--GPALVLVHGFGGNADhwrkNTPVLAKS----HRVYAIDLLGYGYSdkpnprsaPPNSFYTFETWGEQL 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1487551986  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 1487551986  19 IVLVHGLFGSLDNLGVLARDLV-NDHNIIQVDMRNHGLSPRDP-VMNYPAM--AQDLVDTL------DAQQIdkaTFIGH 88
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRLAeLGFNVLAFDYRGYGESEGEPrEEGSPERrdARAAVDYLrtlpgvDPERI---GLLGI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986  89 SMGGkaVMALTALASDRIDKLVAIDIAPVDYhvrrhdeifaainavsesDAQTRQQAAAIMRQHLneeGVIQFL----LK 164
Cdd:COG1073   117 SLGG--GYALNAAATDPRVKAVILDSPFTSL------------------EDLAAQRAKEARGAYL---PGVPYLpnvrLA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1487551986 165 SFVDGEWRfnvPVlwdqyphivgwEKIPAWDHPALFIPGGNSPYVSEQYRDDLLAQFPQARA-HVIAGAGH----WVHAE 239
Cdd:COG1073   174 SLLNDEFD---PL-----------AKIEKISRPLLFIHGEKDEAVPFYMSEDLYEAAAEPKElLIVPGAGHvdlyDRPEE 239

                         250
                  ....*....|....
gi 1487551986 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 1487551986  19 IVLVHGLFGSLDNLGVLARDLVndHNIIQV---DMRNHGLSP--RDPVMNYPAMAQDL---VDTLDAQQIDKATFI-GHS 89
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALA--AQGFAVyayDHRGHGRSDgkRGHVPSFDDYVDDLdtfVDKIREEHPGLPLFLlGHS 84

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1487551986  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 1487551986  19 IVLVHGLFGSLDN-LGVLarDLVNDHNIIQVDMRNHGLSPRDPVMNYPAMAQDLVDTLDAQQIDKATFIGHSMGGKAVM- 96
Cdd:PRK11126    5 LVFLHGLLGSGQDwQPVG--EALPDYPRLYIDLPGHGGSAAISVDGFADVSRLLSQTLQSYNILPYWLVGYSLGGRIAMy 82


                  ....*....
gi 1487551986  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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