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Conserved domains on  [gi|1592100636|ref|WP_132016264|]
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alpha/beta fold hydrolase [Hydrogenispora ethanolica]

Protein Classification

alpha/beta fold hydrolase( domain architecture ID 11426811)

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

PubMed:  1409539|12369917

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-281 8.87e-34

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: 122.42  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  52 DAPPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKLEKASLLGISLGA 131
Cdd:COG0596    22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 132 WLSTKFSVCYPEKVDKLVLLCPAgigpqrISFLFKALFYMLFGEKGMAELYKKINGNQPLPevvlkyqkllgknfnfrre 211
Cdd:COG0596   101 MVALELAARHPERVAGLVLVDEV------LAALAEPLRRPGLAPEALAALLRALARTDLRE------------------- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592100636 212 viplfsdlELKQLSMPVILFVGEKDIMLhSAVTAKRLGDLLPHAKINVLPGAGHTLIN-----LTDRISAFLASN 281
Cdd:COG0596   156 --------RLARITVPTLVIWGEKDPIV-PPALARRLAELLPNAELVVLPGAGHFPPLeqpeaFAAALRDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-281 8.87e-34

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: 122.42  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  52 DAPPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKLEKASLLGISLGA 131
Cdd:COG0596    22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 132 WLSTKFSVCYPEKVDKLVLLCPAgigpqrISFLFKALFYMLFGEKGMAELYKKINGNQPLPevvlkyqkllgknfnfrre 211
Cdd:COG0596   101 MVALELAARHPERVAGLVLVDEV------LAALAEPLRRPGLAPEALAALLRALARTDLRE------------------- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592100636 212 viplfsdlELKQLSMPVILFVGEKDIMLhSAVTAKRLGDLLPHAKINVLPGAGHTLIN-----LTDRISAFLASN 281
Cdd:COG0596   156 --------RLARITVPTLVIWGEKDPIV-PPALARRLAELLPNAELVVLPGAGHFPPLeqpeaFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 49-265 1.39e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.53  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  49 GEKDAPPLILLHGSA--FNSMMWIEDSreYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKLEKASLLG 126
Cdd:PRK14875  127 GEGDGTPVVLIHGFGgdLNNWLFNHAA--LAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERAHLVG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 127 ISLGAWLSTKFSVCYPEKVDKLVLLCPAGIGPQrIS--FL-----------FKALFYMLFGEKG-----MAE---LYKKI 185
Cdd:PRK14875  204 HSMGGAVALRLAARAPQRVASLTLIAPAGLGPE-INgdYIdgfvaaesrreLKPVLELLFADPAlvtrqMVEdllKYKRL 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 186 NGnqplpeVVLKYQKLLGKNFNFRREVIPLFSDLElkQLSMPVILFVGEKDimlhSAVTAKRLGDLLPHAKINVLPGAGH 265
Cdd:PRK14875  283 DG------VDDALRALADALFAGGRQRVDLRDRLA--SLAIPVLVIWGEQD----RIIPAAHAQGLPDGVAVHVLPGAGH 350
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 54-265 1.62e-15

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: 74.08  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  54 PPLILLHGSAFNSMMWIEDSREYSRN-YRVYAIDIPGePGRSDE--TQLSFSGPALVEWLLDVFSALKLEKASLLGISLG 130
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRG-FGKSSRpkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 131 AWLSTKFSVCYPEKVDKLVLLCP--------------------------AGIGPQR----ISFLFKALFYMLFGEKGMAE 180
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAldppheldeadrfilalfpgffdgfvADFAPNPlgrlVAKLLALLLLRLRLLKALPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 181 LYKKINGNQPLPEVVLKYQKLLGKNFNFRREVIPLFSdlelkQLSMPVILFVGEKDIMLHSAVTAKrLGDLLPHAKINVL 260
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLG-----RLDEPTLIIWGDQDPLVPPQALEK-LAQLFPNARLVVI 233


                  ....*
gi 1592100636 261 PGAGH 265
Cdd:pfam00561 234 PDAGH 238
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 52-281 8.87e-34

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: 122.42  E-value: 8.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  52 DAPPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKLEKASLLGISLGA 131
Cdd:COG0596    22 DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAGGYTLDDLADDLAALLDALGLERVVLVGHSMGG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 132 WLSTKFSVCYPEKVDKLVLLCPAgigpqrISFLFKALFYMLFGEKGMAELYKKINGNQPLPevvlkyqkllgknfnfrre 211
Cdd:COG0596   101 MVALELAARHPERVAGLVLVDEV------LAALAEPLRRPGLAPEALAALLRALARTDLRE------------------- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1592100636 212 viplfsdlELKQLSMPVILFVGEKDIMLhSAVTAKRLGDLLPHAKINVLPGAGHTLIN-----LTDRISAFLASN 281
Cdd:COG0596   156 --------RLARITVPTLVIWGEKDPIV-PPALARRLAELLPNAELVVLPGAGHFPPLeqpeaFAAALRDFLARL 221
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 49-265 1.39e-17

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 81.53  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  49 GEKDAPPLILLHGSA--FNSMMWIEDSreYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKLEKASLLG 126
Cdd:PRK14875  127 GEGDGTPVVLIHGFGgdLNNWLFNHAA--LAAGRPVIALDLPGH-GASSKAVGAGSLDELAAAVLAFLDALGIERAHLVG 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 127 ISLGAWLSTKFSVCYPEKVDKLVLLCPAGIGPQrIS--FL-----------FKALFYMLFGEKG-----MAE---LYKKI 185
Cdd:PRK14875  204 HSMGGAVALRLAARAPQRVASLTLIAPAGLGPE-INgdYIdgfvaaesrreLKPVLELLFADPAlvtrqMVEdllKYKRL 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 186 NGnqplpeVVLKYQKLLGKNFNFRREVIPLFSDLElkQLSMPVILFVGEKDimlhSAVTAKRLGDLLPHAKINVLPGAGH 265
Cdd:PRK14875  283 DG------VDDALRALADALFAGGRQRVDLRDRLA--SLAIPVLVIWGEQD----RIIPAAHAQGLPDGVAVHVLPGAGH 350
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 54-265 1.62e-15

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: 74.08  E-value: 1.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  54 PPLILLHGSAFNSMMWIEDSREYSRN-YRVYAIDIPGePGRSDE--TQLSFSGPALVEWLLDVFSALKLEKASLLGISLG 130
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRG-FGKSSRpkAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 131 AWLSTKFSVCYPEKVDKLVLLCP--------------------------AGIGPQR----ISFLFKALFYMLFGEKGMAE 180
Cdd:pfam00561  80 GLIALAYAAKYPDRVKALVLLGAldppheldeadrfilalfpgffdgfvADFAPNPlgrlVAKLLALLLLRLRLLKALPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 181 LYKKINGNQPLPEVVLKYQKLLGKNFNFRREVIPLFSdlelkQLSMPVILFVGEKDIMLHSAVTAKrLGDLLPHAKINVL 260
Cdd:pfam00561 160 LNKRFPSGDYALAKSLVTGALLFIETWSTELRAKFLG-----RLDEPTLIIWGDQDPLVPPQALEK-LAQLFPNARLVVI 233


                  ....*
gi 1592100636 261 PGAGH 265
Cdd:pfam00561 234 PDAGH 238
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
54-280 5.41e-15

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 72.34  E-value: 5.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  54 PPLILLHGSAFNSMMWIEDSREYSRN-YRVYAIDIPGEpGRSDETQLSFSG-PALVEWLLDVFSALKLEKAS---LLGIS 128
Cdd:COG2267    29 GTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGH-GRSDGPRGHVDSfDDYVDDLRAALDALRARPGLpvvLLGHS 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 129 LGAWLSTKFSVCYPEKVDKLVLLCPAgigpqrisflfkalfymlfgekgmaelykkiNGNQPLPEVVLKYqkllgknfnf 208
Cdd:COG2267   108 MGGLIALLYAARYPDRVAGLVLLAPA-------------------------------YRADPLLGPSARW---------- 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1592100636 209 rreVIPLFSDLELKQLSMPVILFVGEKDIMLHSAVTAKRLGDLLPHAKINVLPGAGHTLIN------LTDRISAFLAS 280
Cdd:COG2267   147 ---LRALRLAEALARIDVPVLVLHGGADRVVPPEAARRLAARLSPDVELVLLPGARHELLNepareeVLAAILAWLER 221
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 36-247 4.20e-13

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 67.76  E-value: 4.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  36 VKTRYGSTFIIATG--EKDAPPLI------LLHGSAFNSMMWIEDSREYSRNYRVYAIDIPG-----EPGRSDETQLSFS 102
Cdd:pfam03096   4 IETPCGSVHVTVYGdpEGKKPPILtyhdlgLNHKSCFQGLFNSESMQEILENFCIYHVDAPGqedgaASFPGGYPYPSMD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 103 GpaLVEWLLDVFSALKLEKASLLGISLGAWLSTKFSVCYPEKVDKLVLLCPAGIGPQRISFLFKALFYMLFGEKGMAELY 182
Cdd:pfam03096  84 D--LADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLLYYYGMTDSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 183 KKI--------NGNQPLPEVVLKYQKLLG------------KNFNFRReviPLFSDLELKQLSMPVILFVGEKDIMLHSA 242
Cdd:pfam03096 162 KDYllahyfgkEELSNNSDIVQEYRKFLKerlnpknlqlylEAYNSRR---DLTIERPGLETKCPVLLVVGDNSPHVDAV 238


                  ....*
gi 1592100636 243 VTAKR 247
Cdd:pfam03096 239 VECNT 243
PLN02894 PLN02894
hydrolase, alpha/beta fold family protein
 49-159 1.41e-11

hydrolase, alpha/beta fold family protein


Pssm-ID: 215484 [Multi-domain]  Cd Length: 402  Bit Score: 64.16  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  49 GEKDAPPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEPGRSDETQLSFSGPALVEWLLDVFS----ALKLEKASL 124
Cdd:PLN02894  101 SKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDFTCKSTEETEAWFIDSFEewrkAKNLSNFIL 180

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1592100636 125 LGISLGAWLSTKFSVCYPEKVDKLVLLCPAGIGPQ 159
Cdd:PLN02894  181 LGHSFGGYVAAKYALKHPEHVQHLILVGPAGFSSE 215
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 56-265 6.57e-10

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


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 57.87  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  56 LILLHGSAFNSMMWiedSREYSRNYRVYAIDIPGEpGRSDETQLSFSGPALVEWLLDVFSALKleKASLLGISLGAWLST 135
Cdd:pfam12697   1 VVLVHGAGLSAAPL---AALLAAGVAVLAPDLPGH-GSSSPPPLDLADLADLAALLDELGAAR--PVVLVGHSLGGAVAL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 136 KFSvcyPEKVDKLVLLCPAGIGPQRISFLFKALFYMLFGEkGMAELYKKINGNQPLPEVVLKYQKLLGknfnFRREVIPL 215
Cdd:pfam12697  75 AAA---AAALVVGVLVAPLAAPPGLLAALLALLARLGAAL-AAPAWLAAESLARGFLDDLPADAEWAA----ALARLAAL 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1592100636 216 FSDLELKQLS-----MPVILFVGEKDIMLHSAvtAKRLGDLLPHAKINVLPGAGH 265
Cdd:pfam12697 147 LAALALLPLAawrdlPVPVLVLAEEDRLVPEL--AQRLLAALAGARLVVLPGAGH 199
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
57-280 8.61e-10

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 57.64  E-value: 8.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  57 ILLHGsaF----NSMMWIedsREY--SRNYRVYAIDIPGEpGRSDEtQLSFSGPAlvEWLLDV---FSALKL--EKASLL 125
Cdd:COG1647    19 LLLHG--FtgspAEMRPL---AEAlaKAGYTVYAPRLPGH-GTSPE-DLLKTTWE--DWLEDVeeaYEILKAgyDKVIVI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 126 GISLGAWLSTKFSVCYPEkVDKLVLLCPAgIGPQRISFLFKALFYMLfgekgmAELYKKINGNQPLPEV-VLKYQKLLGK 204
Cdd:COG1647    90 GLSMGGLLALLLAARYPD-VAGLVLLSPA-LKIDDPSAPLLPLLKYL------ARSLRGIGSDIEDPEVaEYAYDRTPLR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 205 NF----NFRREVIPlfsdlELKQLSMPVILFVGEKDIMLHSAVT---AKRLGDllPHAKINVLPGAGHTLIN------LT 271
Cdd:COG1647   162 ALaelqRLIREVRR-----DLPKITAPTLIIQSRKDEVVPPESAryiYERLGS--PDKELVWLEDSGHVITLdkdreeVA 234


                  ....*....
gi 1592100636 272 DRISAFLAS 280
Cdd:COG1647   235 EEILDFLER 243
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 56-269 2.32e-09

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: 56.45  E-value: 2.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  56 LILLHGSAfnsmmwiEDSREYS--------RNYRVYAIDI------PGEPGRSDetqlSFSgpALVEWLLDVFSALKLEK 121
Cdd:pfam12146   7 VVLVHGLG-------EHSGRYAhladalaaQGFAVYAYDHrghgrsDGKRGHVP----SFD--DYVDDLDTFVDKIREEH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 122 AS----LLGISLGAWLSTKFSVCYPEKVDKLVLLCPA-GIGPQRISFLFKALFYMLfgekGMAELYKKINGNQPL----- 191
Cdd:pfam12146  74 PGlplfLLGHSMGGLIAALYALRYPDKVDGLILSAPAlKIKPYLAPPILKLLAKLL----GKLFPRLRVPNNLLPdslsr 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 192 -PEVVLKYQK--LLGKNFNFR--REVIPLFSDLE--LKQLSMPVILFVGEKDIMLHSAVTaKRLGDLLPHA--KINVLPG 262
Cdd:pfam12146 150 dPEVVAAYAAdpLVHGGISARtlYELLDAGERLLrrAAAITVPLLLLHGGADRVVDPAGS-REFYERAGSTdkTLKLYPG 228


                  ....*..
gi 1592100636 263 AGHTLIN 269
Cdd:pfam12146 229 LYHELLN 235
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
56-265 4.23e-09

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 55.79  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  56 LILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEpGRSDetqlSFSGPALVEWLLDVFSALKlEKASLLGISLGAWLST 135
Cdd:PRK10349   16 LVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGF-GRSR----GFGALSLADMAEAVLQQAP-DKAIWLGWSLGGLVAS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636 136 KFSVCYPEKVDKLVLLCPA----------GIGP-------QRISFLFKALFYMLFGEKGM--------AELYKKINGNQP 190
Cdd:PRK10349   90 QIALTHPERVQALVTVASSpcfsardewpGIKPdvlagfqQQLSDDFQRTVERFLALQTMgtetarqdARALKKTVLALP 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1592100636 191 LPEV-VLKYQKLLGKNFNFRreviplfsdLELKQLSMPVILFVGEKDIMLHSAVtAKRLGDLLPHAKINVLPGAGH 265
Cdd:PRK10349  170 MPEVdVLNGGLEILKTVDLR---------QPLQNVSMPFLRLYGYLDGLVPRKV-VPMLDKLWPHSESYIFAKAAH 235
PLN02578 PLN02578
hydrolase
 54-155 3.17e-07

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 50.99  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  54 PPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGepgrsdetqLSFSGPALVE-----WLLDVFSALK---LEKASLL 125
Cdd:PLN02578   87 LPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLG---------FGWSDKALIEydamvWRDQVADFVKevvKEPAVLV 157

                          90       100       110
                  ....*....|....*....|....*....|
gi 1592100636 126 GISLGAWLSTKFSVCYPEKVDKLVLLCPAG 155
Cdd:PLN02578  158 GNSLGGFTALSTAVGYPELVAGVALLNSAG 187
PRK10673 PRK10673
esterase;
52-151 1.35e-04

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 42.41  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  52 DAPPLILLHGsAFNSMmwieD-----SREYSRNYRVYAIDIP--GEPGRSDETQLsfsgPALVEWLLDVFSALKLEKASL 124
Cdd:PRK10673   15 NNSPIVLVHG-LFGSL----DnlgvlARDLVNDHDIIQVDMRnhGLSPRDPVMNY----PAMAQDLLDTLDALQIEKATF 85

                          90       100
                  ....*....|....*....|....*..
gi 1592100636 125 LGISLGAWLSTKFSVCYPEKVDKLVLL 151
Cdd:PRK10673   86 IGHSMGGKAVMALTALAPDRIDKLVAI 112
YpfH COG0400
Predicted esterase [General function prediction only];
49-154 1.82e-04

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 41.43  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  49 GEKDAPPLILLHG---SAfNSMMWIedSREYSR-NYRVYAI--------------DIPGEPGRSDETQLSFSGPALVEWL 110
Cdd:COG0400     1 GGPAAPLVVLLHGyggDE-EDLLPL--APELALpGAAVLAPrapvpegpggrawfDLSFLEGREDEEGLAAAAEALAAFI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1592100636 111 LDVFSALKL--EKASLLGISLGAWLSTKFSVCYPEKVDKLVLLCPA 154
Cdd:COG0400    78 DELEARYGIdpERIVLAGFSQGAAMALSLALRRPELLAGVVALSGY 123
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 52-151 1.13e-03

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 39.72  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1592100636  52 DAPPLILLHGSAFNSMMWIEDSREYSRNYRVYAIDIPGEpGRSDETQLSFSGPALV-------EWLLDVFSALKLEKASL 124
Cdd:PLN02824   28 SGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGY-GYSDKPNPRSAPPNSFytfetwgEQLNDFCSDVVGDPAFV 106

                          90       100
                  ....*....|....*....|....*..
gi 1592100636 125 LGISLGAWLSTKFSVCYPEKVDKLVLL 151
Cdd:PLN02824  107 ICNSVGGVVGLQAAVDAPELVRGVMLI 133
 
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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