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Conserved domains on  [gi|1517860074|gb|ROZ60900|]
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alpha/beta hydrolase [Rhodococcus sp. WS1]

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, ...
 3-244 5.89e-42

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: 142.45  E-value: 5.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   3 HDEGGTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGR--PAPSELTTEAFVDDLASAVASIE-EPMIVIGH 79
Cdd:COG0596    17 REAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRsdKPAGGYTLDDLADDLAALLDALGlERVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  80 SMGALHAWCFAASHPEKVCALVLEDMAPDFrgrtAADWAQMISAWPQPFASedamkeffgpvagqyFLDSFDRRDdgwyl 159
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVLAA----LAEPLRRPGLAPEALAA---------------LLRALARTD----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 160 hgevstfrdiseewgtrhFWDQWKAIDVPTLLIEGEF-TITPEGQMREMAER-PGTRYVRIADAGHLVHDDQPQRYREVV 237
Cdd:COG0596   153 ------------------LRERLARITVPTLVIWGEKdPIVPPALARRLAELlPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*..
gi 1517860074 238 TEFLQTV 244
Cdd:COG0596   215 RDFLARL 221
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-244 5.89e-42

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: 142.45  E-value: 5.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   3 HDEGGTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGR--PAPSELTTEAFVDDLASAVASIE-EPMIVIGH 79
Cdd:COG0596    17 REAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRsdKPAGGYTLDDLADDLAALLDALGlERVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  80 SMGALHAWCFAASHPEKVCALVLEDMAPDFrgrtAADWAQMISAWPQPFASedamkeffgpvagqyFLDSFDRRDdgwyl 159
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVLAA----LAEPLRRPGLAPEALAA---------------LLRALARTD----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 160 hgevstfrdiseewgtrhFWDQWKAIDVPTLLIEGEF-TITPEGQMREMAER-PGTRYVRIADAGHLVHDDQPQRYREVV 237
Cdd:COG0596   153 ------------------LRERLARITVPTLVIWGEKdPIVPPALARRLAELlPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*..
gi 1517860074 238 TEFLQTV 244
Cdd:COG0596   215 RDFLARL 221
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 11-230 5.25e-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: 91.03  E-value: 5.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  11 PILLLHGLMGSSRTWRRQVPWIREFGH-VYTFDAAGHGR----PAPSELTTEAFVDDLASAV-ASIEEPMIVIGHSMGAL 84
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFrVIALDLRGFGKssrpKAQDDYRTDDLAEDLEYILeALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  85 HAWCFAASHPEKVCALVLED------MAPDFRGRTAADWAQMISAWPQPFA-------SEDAMKEFFGPVAGQYFLDSFD 151
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGaldpphELDEADRFILALFPGFFDGFVADFApnplgrlVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 152 RR--DDGWYLHGEVSTFRDIS-EEWGTRHFWDQWKAIDVPTLLIEGEFT-ITPEGQMREMAER-PGTRYVRIADAGHLVH 226
Cdd:pfam00561 162 KRfpSGDYALAKSLVTGALLFiETWSTELRAKFLGRLDEPTLIIWGDQDpLVPPQALEKLAQLfPNARLVVIPDAGHFAF 241


                  ....
gi 1517860074 227 DDQP 230
Cdd:pfam00561 242 LEGP 245
PLN02578 PLN02578
hydrolase
 7-109 2.67e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 56.39  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   7 GTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRPAPSELTTEAFV--DDLASAVASI-EEPMIVIGHSMGA 83
Cdd:PLN02578   84 GEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVwrDQVADFVKEVvKEPAVLVGNSLGG 163

                          90       100
                  ....*....|....*....|....*.
gi 1517860074  84 LHAWCFAASHPEKVCALVLEDMAPDF 109
Cdd:PLN02578  164 FTALSTAVGYPELVAGVALLNSAGQF 189
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-123 1.60e-07

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 50.59  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  10 QPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRpapSELTTEAFVDDLASAVAS-IEEPMIVIGHSMGALHAWC 88
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR---SRGFGPLSLADMAEAIAAqAPDPAIWLGWSLGGLVALH 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1517860074  89 FAASHPEKVCALVLEDMAPDFRGRtaADWAQMISA 123
Cdd:TIGR01738  82 IAATHPDRVRALVTVASSPCFSAR--EDWPEGIKP 114
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 56-110 7.21e-05

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


Pssm-ID: 214008  Cd Length: 280  Bit Score: 42.98  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1517860074  56 TEAFVDDLASAVASIEEPMIVIGHSMGALHAWCFAASHPEKVCALV-LEDMAPDFR 110
Cdd:cd12809   155 QEALVRAAGCALLDIIGPAILITHSQGGPFGWLAADARPDLVKAIVaIEPSGPPFN 210
 
Name Accession Description Interval E-value
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 3-244 5.89e-42

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: 142.45  E-value: 5.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   3 HDEGGTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGR--PAPSELTTEAFVDDLASAVASIE-EPMIVIGH 79
Cdd:COG0596    17 REAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRsdKPAGGYTLDDLADDLAALLDALGlERVVLVGH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  80 SMGALHAWCFAASHPEKVCALVLEDMAPDFrgrtAADWAQMISAWPQPFASedamkeffgpvagqyFLDSFDRRDdgwyl 159
Cdd:COG0596    97 SMGGMVALELAARHPERVAGLVLVDEVLAA----LAEPLRRPGLAPEALAA---------------LLRALARTD----- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 160 hgevstfrdiseewgtrhFWDQWKAIDVPTLLIEGEF-TITPEGQMREMAER-PGTRYVRIADAGHLVHDDQPQRYREVV 237
Cdd:COG0596   153 ------------------LRERLARITVPTLVIWGEKdPIVPPALARRLAELlPNAELVVLPGAGHFPPLEQPEAFAAAL 214


                  ....*..
gi 1517860074 238 TEFLQTV 244
Cdd:COG0596   215 RDFLARL 221
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
5-242 2.17e-22

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 91.22  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   5 EGGTGQPILLLHGLMGSSRTWRRQVPWIREFG-HVYTFDAAGHG---RPAPSELTTEAFVDDLASAVASIEE----PMIV 76
Cdd:COG2267    24 AGSPRGTVVLVHGLGEHSGRYAELAEALAAAGyAVLAFDLRGHGrsdGPRGHVDSFDDYVDDLRAALDALRArpglPVVL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  77 IGHSMGALHAWCFAASHPEKVCALVLedMAPDFRgrtaadwaqmisAWPQPFASEDAMKEFfgpvagqyfldsfdrrddg 156
Cdd:COG2267   104 LGHSMGGLIALLYAARYPDRVAGLVL--LAPAYR------------ADPLLGPSARWLRAL------------------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 157 wylhgevstfrdiseewgtrHFWDQWKAIDVPTLLIEGEF-TITPEGQMREMAER--PGTRYVRIADAGH-LVHDDQPQR 232
Cdd:COG2267   151 --------------------RLAEALARIDVPVLVLHGGAdRVVPPEAARRLAARlsPDVELVLLPGARHeLLNEPAREE 210

                         250
                  ....*....|
gi 1517860074 233 YREVVTEFLQ 242
Cdd:COG2267   211 VLAAILAWLE 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 11-230 5.25e-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: 91.03  E-value: 5.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  11 PILLLHGLMGSSRTWRRQVPWIREFGH-VYTFDAAGHGR----PAPSELTTEAFVDDLASAV-ASIEEPMIVIGHSMGAL 84
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPALARDGFrVIALDLRGFGKssrpKAQDDYRTDDLAEDLEYILeALGLEKVNLVGHSMGGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  85 HAWCFAASHPEKVCALVLED------MAPDFRGRTAADWAQMISAWPQPFA-------SEDAMKEFFGPVAGQYFLDSFD 151
Cdd:pfam00561  82 IALAYAAKYPDRVKALVLLGaldpphELDEADRFILALFPGFFDGFVADFApnplgrlVAKLLALLLLRLRLLKALPLLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 152 RR--DDGWYLHGEVSTFRDIS-EEWGTRHFWDQWKAIDVPTLLIEGEFT-ITPEGQMREMAER-PGTRYVRIADAGHLVH 226
Cdd:pfam00561 162 KRfpSGDYALAKSLVTGALLFiETWSTELRAKFLGRLDEPTLIIWGDQDpLVPPQALEKLAQLfPNARLVVIPDAGHFAF 241


                  ....
gi 1517860074 227 DDQP 230
Cdd:pfam00561 242 LEGP 245
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
7-245 1.22e-16

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 76.52  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   7 GTGQPILLLHGLMGSSRTWRRQVPWIREFG-HVYTFDAAGHGRP--APSELTTEAFVDDLASAVASIE---EPMIVIGHS 80
Cdd:COG1647    13 GGRKGVLLLHGFTGSPAEMRPLAEALAKAGyTVYAPRLPGHGTSpeDLLKTTWEDWLEDVEEAYEILKagyDKVIVIGLS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  81 MG---ALHAwcfAASHPEkVCALVLedMAP--DFRGRTA--ADWAQMISAWPQPFASEDAMKEffgpvagqyfldsfdrR 153
Cdd:COG1647    93 MGgllALLL---AARYPD-VAGLVL--LSPalKIDDPSAplLPLLKYLARSLRGIGSDIEDPE----------------V 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 154 DDGWYLHGEVSTFRDIseEWGTRHFWDQWKAIDVPTLLIEGEF-TITPEGQMREMAER---PGTRYVRIADAGHLVH-DD 228
Cdd:COG1647   151 AEYAYDRTPLRALAEL--QRLIREVRRDLPKITAPTLIIQSRKdEVVPPESARYIYERlgsPDKELVWLEDSGHVITlDK 228

                         250
                  ....*....|....*..
gi 1517860074 229 QPQRYREVVTEFLQTVS 245
Cdd:COG1647   229 DREEVAEEILDFLERLA 245
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 12-236 5.53e-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: 65.96  E-value: 5.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  12 ILLLHGLMGSSRTWRRQVpwiREFGHVYTFDAAGHGRPAPSELTTEAfVDDLASAVASI--EEPMIVIGHSMGALHAWcf 89
Cdd:pfam12697   1 VVLVHGAGLSAAPLAALL---AAGVAVLAPDLPGHGSSSPPPLDLAD-LADLAALLDELgaARPVVLVGHSLGGAVAL-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  90 AASHPEKVCALVLEDMAPDFrgrtaaDWAQMISAWPQPFASEDAMKEFF-GPVAGQYFLDSFDRRDDGWYLHGEVSTFRD 168
Cdd:pfam12697  75 AAAAAALVVGVLVAPLAAPP------GLLAALLALLARLGAALAAPAWLaAESLARGFLDDLPADAEWAAALARLAALLA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1517860074 169 ISEEWGTRHfwdqWKAIDVPTLLIEGEFTITPEGQMREMAERPGTRYVRIADAGHLVHdDQPQRYREV 236
Cdd:pfam12697 149 ALALLPLAA----WRDLPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAEA 211
EstA COG1075
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ...
 8-101 1.47e-10

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


Pssm-ID: 440693 [Multi-domain]  Cd Length: 106  Bit Score: 56.76  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   8 TGQPILLLHGLMGSSRTWRRQVPWIREFGH-VYTFDAAGHGRPapseltTEAFVDDLASAVASI-----EEPMIVIGHSM 81
Cdd:COG1075     4 TRYPVVLVHGLGGSAASWAPLAPRLRAAGYpVYALNYPSTNGS------IEDSAEQLAAFVDAVlaatgAEKVDLVGHSM 77

                          90       100
                  ....*....|....*....|..
gi 1517860074  82 GALHAWCFAASH--PEKVCALV 101
Cdd:COG1075    78 GGLVARYYLKRLggAAKVARVV 99
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 12-243 2.73e-10

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 58.77  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  12 ILLLHGLMGSSRTWRRQVPWIREFG-HVYTFDAAGHG-----------------RPAPSELTTEAFVDDlasavasieEP 73
Cdd:COG1073    40 VVVAHGNGGVKEQRALYAQRLAELGfNVLAFDYRGYGesegepreegsperrdaRAAVDYLRTLPGVDP---------ER 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  74 MIVIGHSMGALHAWCFAASHPEkVCALVLE----DMAPDFRGRTAADWAQMISAWPqpfasedamkefFGPVAGqyfLDS 149
Cdd:COG1073   111 IGLLGISLGGGYALNAAATDPR-VKAVILDspftSLEDLAAQRAKEARGAYLPGVP------------YLPNVR---LAS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 150 FdrrddgwyLHGEVSTFRDISEewgtrhfwdqwkaIDVPTLLIEGE-FTITPEGQMREMAER--PGTRYVRIADAGH-LV 225
Cdd:COG1073   175 L--------LNDEFDPLAKIEK-------------ISRPLLFIHGEkDEAVPFYMSEDLYEAaaEPKELLIVPGAGHvDL 233

                         250
                  ....*....|....*...
gi 1517860074 226 HDDQPQRYREVVTEFLQT 243
Cdd:COG1073   234 YDRPEEEYFDKLAEFFKK 251
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 12-113 2.95e-10

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: 58.38  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  12 ILLLHGLMGSSRTWRRQVPWIREFG-HVYTFDAAGHGR--PAPSELT-TEAFVDDLASAVASI-----EEPMIVIGHSMG 82
Cdd:pfam12146   7 VVLVHGLGEHSGRYAHLADALAAQGfAVYAYDHRGHGRsdGKRGHVPsFDDYVDDLDTFVDKIreehpGLPLFLLGHSMG 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1517860074  83 ALHAWCFAASHPEKVCALVLEdmAPDFRGRT 113
Cdd:pfam12146  87 GLIAALYALRYPDKVDGLILS--APALKIKP 115
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-241 1.08e-09

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 56.95  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  12 ILLLHGLMGS-SRTWRRQVPWIREFG-HVYTFDAAGHGRPAPSELTTEafVDDLASAVAS-IEEPMI------VIGHSMG 82
Cdd:COG1506    26 VVYVHGGPGSrDDSFLPLAQALASRGyAVLAPDYRGYGESAGDWGGDE--VDDVLAAIDYlAARPYVdpdrigIYGHSYG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  83 ALHAWCFAASHPEKVCALVLEDMAPDFRGRTAADWAQMISAWPQPFASEDAMKEFfgpvagqyfldsfdrrddgwylhge 162
Cdd:COG1506   104 GYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTREYTERLMGGPWEDPEAYAAR------------------------- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 163 vSTFRDIseewgtrhfwdqwKAIDVPTLLIEGEF-TITPEGQMREMAER-----PGTRYVRIADAGHLVHDDQPQRYREV 236
Cdd:COG1506   159 -SPLAYA-------------DKLKTPLLLIHGEAdDRVPPEQAERLYEAlkkagKPVELLVYPGEGHGFSGAGAPDYLER 224


                  ....*
gi 1517860074 237 VTEFL 241
Cdd:COG1506   225 ILDFL 229
PLN02578 PLN02578
hydrolase
 7-109 2.67e-09

hydrolase


Pssm-ID: 215315 [Multi-domain]  Cd Length: 354  Bit Score: 56.39  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   7 GTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRPAPSELTTEAFV--DDLASAVASI-EEPMIVIGHSMGA 83
Cdd:PLN02578   84 GEGLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSDKALIEYDAMVwrDQVADFVKEVvKEPAVLVGNSLGG 163

                          90       100
                  ....*....|....*....|....*.
gi 1517860074  84 LHAWCFAASHPEKVCALVLEDMAPDF 109
Cdd:PLN02578  164 FTALSTAVGYPELVAGVALLNSAGQF 189
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 7-102 5.90e-09

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 55.72  E-value: 5.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   7 GTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRPAP-------SEL--TTEAFVDDLASAVAsieepmIVI 77
Cdd:PRK14875  129 GDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKavgagslDELaaAVLAFLDALGIERA------HLV 202

                          90       100
                  ....*....|....*....|....*
gi 1517860074  78 GHSMGALHAWCFAASHPEKVCALVL 102
Cdd:PRK14875  203 GHSMGGAVALRLAARAPQRVASLTL 227
PLN02824 PLN02824
hydrolase, alpha/beta fold family protein
 6-142 1.30e-08

hydrolase, alpha/beta fold family protein


Pssm-ID: 178419 [Multi-domain]  Cd Length: 294  Bit Score: 54.36  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   6 GGTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHG---RPAPSELTTEAF---------VDDLASAVasIEEP 73
Cdd:PLN02824   26 GTSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGysdKPNPRSAPPNSFytfetwgeqLNDFCSDV--VGDP 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1517860074  74 MIVIGHSMGALHAWCFAASHPEKVCALVLedMAPDFRG---RTAADWAQ-MISAWPQPFASEDAMKEFFGPVA 142
Cdd:PLN02824  104 AFVICNSVGGVVGLQAAVDAPELVRGVML--INISLRGlhiKKQPWLGRpFIKAFQNLLRETAVGKAFFKSVA 174
PRK10673 PRK10673
esterase;
11-243 1.06e-07

esterase;


Pssm-ID: 182637 [Multi-domain]  Cd Length: 255  Bit Score: 51.27  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  11 PILLLHGLMGS-------SRTWRRQVPWIRefghvytFDAAGHG-RPAPSELTTEAFVDDLASAVASIE-EPMIVIGHSM 81
Cdd:PRK10673   18 PIVLVHGLFGSldnlgvlARDLVNDHDIIQ-------VDMRNHGlSPRDPVMNYPAMAQDLLDTLDALQiEKATFIGHSM 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  82 GALHAWCFAASHPEKVCALVLEDMAP-DFRGRT-----AADWAQMISAWPQPFASEDAMKEFF---GPVagQYFLDSFdr 152
Cdd:PRK10673   91 GGKAVMALTALAPDRIDKLVAIDIAPvDYHVRRhdeifAAINAVSEAGATTRQQAAAIMRQHLneeGVI--QFLLKSF-- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 153 RDDGWYLHGEVstfrdiseewgtrhFWDQ------WKAI---DVPTLLIEGEFTITPEGQMRE--MAERPGTRYVRIADA 221
Cdd:PRK10673  167 VDGEWRFNVPV--------------LWDQyphivgWEKIpawPHPALFIRGGNSPYVTEAYRDdlLAQFPQARAHVIAGA 232

                         250       260
                  ....*....|....*....|..
gi 1517860074 222 GHLVHDDQPQRYREVVTEFLQT 243
Cdd:PRK10673  233 GHWVHAEKPDAVLRAIRRYLND 254
bioH TIGR01738
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ...
 10-123 1.60e-07

pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273783 [Multi-domain]  Cd Length: 245  Bit Score: 50.59  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  10 QPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRpapSELTTEAFVDDLASAVAS-IEEPMIVIGHSMGALHAWC 88
Cdd:TIGR01738   5 VHLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGR---SRGFGPLSLADMAEAIAAqAPDPAIWLGWSLGGLVALH 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1517860074  89 FAASHPEKVCALVLEDMAPDFRGRtaADWAQMISA 123
Cdd:TIGR01738  82 IAATHPDRVRALVTVASSPCFSAR--EDWPEGIKP 114
PRK11126 PRK11126
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
 9-242 4.10e-06

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


Pssm-ID: 236855 [Multi-domain]  Cd Length: 242  Bit Score: 46.37  E-value: 4.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   9 GQPIL-LLHGLMGSSRTWRRQVPWIREFgHVYTFDAAGHGRpapSELTTeafVDDLASAVASIEE--------PMIVIGH 79
Cdd:PRK11126    1 GLPWLvFLHGLLGSGQDWQPVGEALPDY-PRLYIDLPGHGG---SAAIS---VDGFADVSRLLSQtlqsynilPYWLVGY 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  80 SMG---ALHAWCFaaSHPEKVCALVLE--------DMAPDFRGRTAADWAQMisawpqpFASEdamkeffgPVAgQYFLD 148
Cdd:PRK11126   74 SLGgriAMYYACQ--GLAGGLCGLIVEggnpglqnAEERQARWQNDRQWAQR-------FRQE--------PLE-QVLAD 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 149 sfdrrddgWYlhgEVSTFRDISEE------------------------------WgtrhFWDQWKAIDVPTLLIEGE--- 195
Cdd:PRK11126  136 --------WY---QQPVFASLNAEqrqqlvakrsnnngaavaamleatslakqpD----LRPALQALTFPFYYLCGErds 200

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1517860074 196 -FtitpegqmREMAERPGTRYVRIADAGHLVHDDQPQRYREVVTEFLQ 242
Cdd:PRK11126  201 kF--------QALAQQLALPLHVIPNAGHNAHRENPAAFAASLAQILR 240
PLN02679 PLN02679
hydrolase, alpha/beta fold family protein
 9-102 4.99e-06

hydrolase, alpha/beta fold family protein


Pssm-ID: 178283 [Multi-domain]  Cd Length: 360  Bit Score: 46.76  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   9 GQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHG---RPAPSELTTEA-------FVDDLasavasIEEPMIVIG 78
Cdd:PLN02679   88 GPPVLLVHGFGASIPHWRRNIGVLAKNYTVYAIDLLGFGasdKPPGFSYTMETwaelildFLEEV------VQKPTVLIG 161

                          90       100
                  ....*....|....*....|....*.
gi 1517860074  79 HSMGALhAWCFAA--SHPEKVCALVL 102
Cdd:PLN02679  162 NSVGSL-ACVIAAseSTRDLVRGLVL 186
PRK05855 PRK05855
SDR family oxidoreductase;
3-87 6.57e-06

SDR family oxidoreductase;


Pssm-ID: 235628 [Multi-domain]  Cd Length: 582  Bit Score: 46.51  E-value: 6.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   3 HDEGGTGQPILLL-HGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGR---PAP-SELTTEAFVDDLAsAVA---SIEEPM 74
Cdd:PRK05855   18 YEWGDPDRPTVVLvHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRssaPKRtAAYTLARLADDFA-AVIdavSPDRPV 96

                          90
                  ....*....|...
gi 1517860074  75 IVIGHSMGALHAW 87
Cdd:PRK05855   97 HLLAHDWGSIQGW 109
PRK03592 PRK03592
haloalkane dehalogenase; Provisional
 1-245 2.80e-05

haloalkane dehalogenase; Provisional


Pssm-ID: 235135  Cd Length: 295  Bit Score: 44.21  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   1 MLHDEGGTGQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRPAPSELTTeAFVDDLASAVASIE----EPMIV 76
Cdd:PRK03592   19 MAYIETGEGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASDKPDIDY-TFADHARYLDAWFDalglDDVVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  77 IGHSMGALHAWCFAASHPEKVCALVL----------EDMAPDFRG-----RTAADWAQMI--------SAWPQPFA---S 130
Cdd:PRK03592   98 VGHDWGSALGFDWAARHPDRVRGIAFmeaivrpmtwDDFPPAVRElfqalRSPGEGEEMVleenvfieRVLPGSILrplS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 131 EDAMKEFFGPvagqyFLDSFDRRDDGWY-----LHGEVSTFRDISEEwgtrhfWDQW-KAIDVPTLLIEGE-FTITPEGQ 203
Cdd:PRK03592  178 DEEMAVYRRP-----FPTPESRRPTLSWprelpIDGEPADVVALVEE------YAQWlATSDVPKLLINAEpGAILTTGA 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1517860074 204 MREMAER--PGTRYVRIADAGHLVHDDQPQRYREVVTEFLQTVS 245
Cdd:PRK03592  247 IRDWCRSwpNQLEITVFGAGLHFAQEDSPEEIGAAIAAWLRRLR 290
Esterase_713_like-2 cd12809
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ...
 56-110 7.21e-05

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


Pssm-ID: 214008  Cd Length: 280  Bit Score: 42.98  E-value: 7.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1517860074  56 TEAFVDDLASAVASIEEPMIVIGHSMGALHAWCFAASHPEKVCALV-LEDMAPDFR 110
Cdd:cd12809   155 QEALVRAAGCALLDIIGPAILITHSQGGPFGWLAADARPDLVKAIVaIEPSGPPFN 210
PLN03084 PLN03084
alpha/beta hydrolase fold protein; Provisional
 5-102 2.09e-04

alpha/beta hydrolase fold protein; Provisional


Pssm-ID: 178633  Cd Length: 383  Bit Score: 41.79  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   5 EGGT--GQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHG---RPAPS---ELTTEAFVDDLAS---AVASIEEP 73
Cdd:PLN03084  121 ESGSnnNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGfsdKPQPGygfNYTLDEYVSSLESlidELKSDKVS 200

                          90       100
                  ....*....|....*....|....*....
gi 1517860074  74 MIVIGHSMGALHAwcFAASHPEKVCALVL 102
Cdd:PLN03084  201 LVVQGYFSPPVVK--YASAHPDKIKKLIL 227
PLN02980 PLN02980
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ...
 2-241 2.52e-04

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


Pssm-ID: 215530 [Multi-domain]  Cd Length: 1655  Bit Score: 42.15  E-value: 2.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074    2 LHDEGGT--GQPILLLHGLMGSSRTWRRQVPWIREFGHVYTFDAAGHGRP----------APSELTTEAFVDDLASAVAS 69
Cdd:PLN02980  1362 VHEVGQNaeGSVVLFLHGFLGTGEDWIPIMKAISGSARCISIDLPGHGGSkiqnhaketqTEPTLSVELVADLLYKLIEH 1441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   70 IEEPMIVI-GHSMGALHAWCFAASHPEKVCALVLEDMAPDFRGrtaaDWAQMISawpqpFASEDAMKEFFGPVAGQYFLD 148
Cdd:PLN02980  1442 ITPGKVTLvGYSMGARIALYMALRFSDKIEGAVIISGSPGLKD----EVARKIR-----SAKDDSRARMLIDHGLEIFLE 1512

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  149 SfdrrddgWY----------------------LHGEVSTFRDISEEWGT---RHFWDQWKAIDVPTLLIEGE----FTIT 199
Cdd:PLN02980  1513 N-------WYsgelwkslrnhphfnkivasrlLHKDVPSLAKLLSDLSIgrqPSLWEDLKQCDTPLLLVVGEkdvkFKQI 1585

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1517860074  200 PEGQMREMAERPGTR---------YVRIADAGHLVHDDQPQRYREVVTEFL 241
Cdd:PLN02980  1586 AQKMYREIGKSKESGndkgkeiieIVEIPNCGHAVHLENPLPVIRALRKFL 1636
COG4757 COG4757
Predicted alpha/beta hydrolase [General function prediction only];
7-102 6.81e-04

Predicted alpha/beta hydrolase [General function prediction only];


Pssm-ID: 443790 [Multi-domain]  Cd Length: 289  Bit Score: 39.87  E-value: 6.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074   7 GTGQPILLLHGLMG-SSRTWRRQVPWIREFG-HVYTFDAAGHGRPAPSEL------TTEAFVDDLASAVASIEE-----P 73
Cdd:COG4757    29 GPPRAVVLINPATGvPQRFYRPFARYLAERGfAVLTYDYRGIGLSRPGSLrgfdagYRDWGELDLPAVLDALRArfpglP 108

                          90       100
                  ....*....|....*....|....*....
gi 1517860074  74 MIVIGHSMGALHAwCFAASHpEKVCALVL 102
Cdd:COG4757   109 LLLVGHSLGGQLL-GLAPNA-ERVDRLVT 135
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 38-242 1.23e-03

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: 39.26  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  38 VYTFDAAGHGRPAPSELTTEAF--VDDLASAVASIE-----EPMIVIGHSMGALHAWCFAASHPEKVCALVLedMAPDFR 110
Cdd:pfam03096  58 IYHVDAPGQEDGAASFPGGYPYpsMDDLADMLPVVLdhfrlKSVIGMGVGAGAYILARFALKHPERVEGLVL--INPTPK 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 111 GRTAADWA--QMISAWPQPFASEDAMKEFF----------------------------GPVAGQYFLDSFDRRddgwylh 160
Cdd:pfam03096 136 AAGWIEWFynKLSSKLLYYYGMTDSAKDYLlahyfgkeelsnnsdivqeyrkflkerlNPKNLQLYLEAYNSR------- 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 161 gevstfRDISEEWGTrhfwdqwKAIDVPTLLIEGEFTITPEG--QMREMAERPGTRYVRIADAGHLVHDDQPQRYREVVT 238
Cdd:pfam03096 209 ------RDLTIERPG-------LETKCPVLLVVGDNSPHVDAvvECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFK 275


                  ....
gi 1517860074 239 EFLQ 242
Cdd:pfam03096 276 LFLQ 279
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
12-112 1.63e-03

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 38.85  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  12 ILLLHGLMGSSRTWRrqvpWIRE-FGHVYTF---DAAGHGRPAPSELTTeafVDDLASAVA-SIEEPMIVIGHSMGALHA 86
Cdd:PRK10349   16 LVLLHGWGLNAEVWR----CIDEeLSSHFTLhlvDLPGFGRSRGFGALS---LADMAEAVLqQAPDKAIWLGWSLGGLVA 88

                          90       100
                  ....*....|....*....|....*.
gi 1517860074  87 WCFAASHPEKVCALVLEDMAPDFRGR 112
Cdd:PRK10349   89 SQIALTHPERVQALVTVASSPCFSAR 114
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 23-244 2.80e-03

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 37.91  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  23 RTWRRQVP-WIRefghVYTFDAAGHGR----PAPSELttEAFVDDLASAVAS-IEEPMIVIGHSMGALHAWCFA----AS 92
Cdd:COG3208    23 RPWAAALPpDIE----VLAVQLPGRGDrlgePPLTSL--EELADDLAEELAPlLDRPFALFGHSMGALLAFELArrleRR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074  93 HPEKVCALV--------LEDMAPDFRGRTAADWAQMISAW---PQPFASEDAMKEFFGPVAgqyfldsfdRRDdgwylhg 161
Cdd:COG3208    97 GRPLPAHLFvsgrraphLPRRRRPLHDLSDAELLAELRRLggtPEEVLADPELLELFLPIL---------RAD------- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860074 162 evstFRdISEewgtRHFWDQWKAIDVPTLLIEGEF-TITPEGQM---REMAERPGTryVRIADAGHLVHDDQPQRYREVV 237
Cdd:COG3208   161 ----FR-LLE----TYRYTPGPPLDCPITALGGDDdPLVSPEELaawREHTTGPFR--LRVFPGGHFFLRDHPAELLALI 229


                  ....*..
gi 1517860074 238 TEFLQTV 244
Cdd:COG3208   230 RAALAAL 236
PHA02857 PHA02857
monoglyceride lipase; Provisional
 38-107 3.48e-03

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 37.94  E-value: 3.48e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1517860074  38 VYTFDAAGHGRPAPSELTTEAF---VDDLASAVASIEE-----PMIVIGHSMGALHAWCFAASHPEKVCALVLedMAP 107
Cdd:PHA02857   55 VFSHDHIGHGRSNGEKMMIDDFgvyVRDVVQHVVTIKStypgvPVFLLGHSMGATISILAAYKNPNLFTAMIL--MSP 130
 
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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