|
Name |
Accession |
Description |
Interval |
E-value |
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
62-278 |
2.86e-22 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 93.08 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647 11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETETQKEIEMKgewtlpsrynKEGY 219
Cdd:COG1647 89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALK--IDDPSAPLLPLLKYLARSLRGIGSDIEDPEVA----------EYAY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851859573 220 FRIP-------YSFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 278
Cdd:COG1647 156 DRTPlralaelQRLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
|
|
| PLN02578 |
PLN02578 |
hydrolase |
102-164 |
9.81e-07 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 49.45 E-value: 9.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
88-282 |
6.32e-06 |
|
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: 46.44 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146 21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 160 VIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETetqKEIEMKGEWTLPSRYNKEgyfripysfIKEAEHHCLLHSP 239
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPILKLLAKLLGKLFPR---LRVPNNLLPDSLSRDPEV---------VAAYAADPLVHGG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 240 IPV--------------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 282
Cdd:pfam12146 167 ISArtlyelldagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
135-166 |
1.20e-04 |
|
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: 214007 Cd Length: 309 Bit Score: 43.00 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|..
gi 1851859573 135 GPQILVGSSLGGWLMLHAAIARPEKVIALIGI 166
Cdd:cd12808 188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| hydr2_PEP |
TIGR03101 |
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ... |
69-164 |
3.73e-03 |
|
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.
Pssm-ID: 274428 Cd Length: 266 Bit Score: 38.26 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101 28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
|
90 100
....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALI 164
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
62-278 |
2.86e-22 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 93.08 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 62 LKGKTPGIIFIPGYLSNMNGIKAVAveEFCKSLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG--PQIL 139
Cdd:COG1647 11 LEGGRKGVLLLHGFTGSPAEMRPLA--EALAKAGYTVYAPRLPGHGTSPEDLLKTTWEDWLEDVEEAYEILKAGydKVIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 140 VGSSLGGWLMLHAAIARPEkVIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETETQKEIEMKgewtlpsrynKEGY 219
Cdd:COG1647 89 IGLSMGGLLALLLAARYPD-VAGLVLLSPALK--IDDPSAPLLPLLKYLARSLRGIGSDIEDPEVA----------EYAY 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1851859573 220 FRIP-------YSFIKEAEHHclLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVIL 278
Cdd:COG1647 156 DRTPlralaelQRLIREVRRD--LPK---ITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVW 216
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
56-278 |
4.68e-16 |
|
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: 75.42 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 56 NLAYKRLKGKTPGIIFIPGYLSNMNGIKAVAvEEFCKslGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEG 135
Cdd:COG0596 13 RLHYREAGPDGPPVVLLHGLPGSSYEWRPLI-PALAA--GYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 136 PQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADGLVTQYHALPVEVLAYSfnpstwetetqKEIEMKGEWTLPSRYN 215
Cdd:COG0596 90 RVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLAALAEPLRRPGLAPEALA-----------ALLRALARTDLRERLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 216 KegyfripysfikeaehhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIvsPDVDVIL 278
Cdd:COG0596 159 R-------------------------ITVPTLVIWGEKDPIVPPALARRLAELL--PNAELVV 194
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
63-276 |
1.43e-15 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 74.28 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 63 KGKTPGIIFIPGYLSNMNGIKAVAVEEFCkSLGHAFIRFDYSGIGSSDGNLAectvGKWRKDVLSILDDVAEGPQI---- 138
Cdd:COG1506 20 GKKYPVVVYVHGGPGSRDDSFLPLAQALA-SRGYAVLAPDYRGYGESAGDWG----GDEVDDVLAAIDYLAARPYVdpdr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 139 --LVGSSLGGWLMLHAAIARPEKVIALIGIATAADgLVTQYHalpvevlaysfnpstwETETQKEIEMKGEWTLPSRYNK 216
Cdd:COG1506 95 igIYGHSYGGYMALLAAARHPDRFKAAVALAGVSD-LRSYYG----------------TTREYTERLMGGPWEDPEAYAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 217 egyfripYSFIKEAEHhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDV 276
Cdd:COG1506 158 -------RSPLAYADK---------LKTPLLLIHGEADDRVPPEQAERLYEALKKAGKPV 201
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
69-278 |
3.20e-13 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 67.72 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 69 IIFIPGYLSNMNGIKAVAvEEFCKSlGHAFIRFDYSGIGSSDGNLAEC-TVGKWRKDVLSILDDVAE---GPQILVGSSL 144
Cdd:COG2267 31 VVLVHGLGEHSGRYAELA-EALAAA-GYAVLAFDLRGHGRSDGPRGHVdSFDDYVDDLRAALDALRArpgLPVVLLGHSM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 145 GGWLMLHAAIARPEKVIALIGIATaadglvtqyhalpvevlaysfnpstwetetqkeiemkgewtlpsRYNKEGYFRIPY 224
Cdd:COG2267 109 GGLIALLYAARYPDRVAGLVLLAP--------------------------------------------AYRADPLLGPSA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1851859573 225 SFIKEAEHHCLLHSpipVTCPVRLLHGMKDEIVPWQRSLQVADRIvSPDVDVIL 278
Cdd:COG2267 145 RWLRALRLAEALAR---IDVPVLVLHGGADRVVPPEAARRLAARL-SPDVELVL 194
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
63-272 |
2.15e-07 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 51.07 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 63 KGKTPGIIFIPGYLSNMNGIkAVAVEEFCKsLGHAFIRFDYSGIGSSDGNLAEctVGK-WRKDV------LSILDDVAEG 135
Cdd:COG1073 34 SKKYPAVVVAHGNGGVKEQR-ALYAQRLAE-LGFNVLAFDYRGYGESEGEPRE--EGSpERRDAraavdyLRTLPGVDPE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 136 PQILVGSSLGGWLMLHAAIARPEkVIALIGIATAAdglvtqyhalpvevlaysfnpSTWETETQKEIEMKGEWTLPSRYN 215
Cdd:COG1073 110 RIGLLGISLGGGYALNAAATDPR-VKAVILDSPFT---------------------SLEDLAAQRAKEARGAYLPGVPYL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1851859573 216 K----EGYFRIPYSFIKEAEHhcllhspipVTCPVRLLHGMKDEIVPWQRSLQVADRIVSP 272
Cdd:COG1073 168 PnvrlASLLNDEFDPLAKIEK---------ISRPLLFIHGEKDEAVPFYMSEDLYEAAAEP 219
|
|
| PLN02578 |
PLN02578 |
hydrolase |
102-164 |
9.81e-07 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 49.45 E-value: 9.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 102 DYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALI 164
Cdd:PLN02578 119 DLLGFGWSDKALIEYDAMVWRDQVADFVKEVVKEPAVLVGNSLGGFTALSTAVGYPELVAGVA 181
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
88-282 |
6.32e-06 |
|
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: 46.44 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 88 EEFCKSL---GHAFIRFDYSGIGSSDGNLAECT-VGKWRKDVLSILDDVAEG----PQILVGSSLGGWLMLHAAIARPEK 159
Cdd:pfam12146 21 AHLADALaaqGFAVYAYDHRGHGRSDGKRGHVPsFDDYVDDLDTFVDKIREEhpglPLFLLGHSMGGLIAALYALRYPDK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 160 VIALIGIATAADglVTQYHALPVEVLAYSFNPSTWETetqKEIEMKGEWTLPSRYNKEgyfripysfIKEAEHHCLLHSP 239
Cdd:pfam12146 101 VDGLILSAPALK--IKPYLAPPILKLLAKLLGKLFPR---LRVPNNLLPDSLSRDPEV---------VAAYAADPLVHGG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1851859573 240 IPV--------------------TCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILRKQG 282
Cdd:pfam12146 167 ISArtlyelldagerllrraaaiTVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGL 229
|
|
| Peptidase_S9 |
pfam00326 |
Prolyl oligopeptidase family; |
141-279 |
8.91e-05 |
|
Prolyl oligopeptidase family;
Pssm-ID: 459761 [Multi-domain] Cd Length: 213 Bit Score: 42.99 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 141 GSSLGGWLMLHAAIARPEKVIALIGIATAADglVTQYHALPVEVLA--YSFNPSTWetetqkeiemkgewtlpsrYNKEG 218
Cdd:pfam00326 70 GGSYGGYLTGAALNQRPDLFKAAVAHVPVVD--WLAYMSDTSLPFTerYMEWGNPW-------------------DNEEG 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1851859573 219 YFRI-PYSFIKEaehhcllhspIPVTCPVRLLHGMKDEIVPWQRSLQVADRIVSPDVDVILR 279
Cdd:pfam00326 129 YDYLsPYSPADN----------VKVYPPLLLIHGLLDDRVPPWQSLKLVAALQRKGVPFLLL 180
|
|
| COG2945 |
COG2945 |
Alpha/beta superfamily hydrolase [General function prediction only]; |
91-277 |
1.01e-04 |
|
Alpha/beta superfamily hydrolase [General function prediction only];
Pssm-ID: 442188 [Multi-domain] Cd Length: 201 Bit Score: 42.46 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 91 CKSLGHAFIRFDYSGIGSSDGNLAEcTVGKwRKDVLSILDDVAE---GPQILVGSSLGGWLMLHAAIARPEkVIALIGIA 167
Cdd:COG2945 51 LVAAGFAVLRFNFRGVGRSEGEFDE-GRGE-LDDAAAALDWLRAqnpLPLWLAGFSFGAYVALQLAMRLPE-VEGLILVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 168 TAAdglvtqyhalpvevlaysfnpstwetetqkeiemkgewtlpSRYnkegyfriPYSFIKeaehhcllhspiPVTCPVR 247
Cdd:COG2945 128 PPV-----------------------------------------NRY--------DFSFLA------------PCPAPTL 146
|
170 180 190
....*....|....*....|....*....|
gi 1851859573 248 LLHGMKDEIVPWQRSLQVADRiVSPDVDVI 277
Cdd:COG2945 147 VIHGEQDEVVPPAEVLDWARP-LSPPLPVV 175
|
|
| Esterase_713_like-1 |
cd12808 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
135-166 |
1.20e-04 |
|
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: 214007 Cd Length: 309 Bit Score: 43.00 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|..
gi 1851859573 135 GPQILVGSSLGGWLMLHAAIARPEKVIALIGI 166
Cdd:cd12808 188 GPCIVVAHSQGGGFAFEAARARPDLVRAVVAL 219
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
69-194 |
2.02e-04 |
|
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: 42.11 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 69 IIFIPGYLSNMNG----IKAVAveefckSLGHAFIRFDYSGIGSSDGNLAECTVGKW--RKDVLSILDDVAEGPQILVGS 142
Cdd:pfam00561 3 VLLLHGLPGSSDLwrklAPALA------RDGFRVIALDLRGFGKSSRPKAQDDYRTDdlAEDLEYILEALGLEKVNLVGH 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALIGIATAADGlvtqyHALPVEVLAYSFNPSTW 194
Cdd:pfam00561 77 SMGGLIALAYAAKYPDRVKALVLLGALDPP-----HELDEADRFILALFPGF 123
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
69-173 |
7.20e-04 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 40.15 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 69 IIFIPGYlsnmnGIKAVAVEEFCKSlGHAFIRFDYSGIGSSDGNLAECTVgkwRKDVLSILDDVAEGPQ-ILVGSSLGGW 147
Cdd:pfam12697 1 VVLVHGA-----GLSAAPLAALLAA-GVAVLAPDLPGHGSSSPPPLDLAD---LADLAALLDELGAARPvVLVGHSLGGA 71
|
90 100
....*....|....*....|....*.
gi 1851859573 148 LMLHAAIARPEKVIALIGIATAADGL 173
Cdd:pfam12697 72 VALAAAAAALVVGVLVAPLAAPPGLL 97
|
|
| COG4757 |
COG4757 |
Predicted alpha/beta hydrolase [General function prediction only]; |
93-161 |
9.69e-04 |
|
Predicted alpha/beta hydrolase [General function prediction only];
Pssm-ID: 443790 [Multi-domain] Cd Length: 289 Bit Score: 40.25 E-value: 9.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851859573 93 SLGHAFIRFDYSGIGSS-DGNLAECTVGK--W-RKDVLSILDDVAE----GPQILVGSSLGGWLM-LHAAIARPEKVI 161
Cdd:COG4757 57 ERGFAVLTYDYRGIGLSrPGSLRGFDAGYrdWgELDLPAVLDALRArfpgLPLLLVGHSLGGQLLgLAPNAERVDRLV 134
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
95-172 |
1.00e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 40.31 E-value: 1.00e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1851859573 95 GHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSILDDVAEGPQILVGSSLGGWLMLHAAIARPEKVIALIGIATAADG 172
Cdd:PRK14875 157 GRPVIALDLPGHGASSKAVGAGSLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAPAGLG 234
|
|
| hydr2_PEP |
TIGR03101 |
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha ... |
69-164 |
3.73e-03 |
|
exosortase A system-associated hydrolase 2; This group of proteins are members of the alpha/beta hydrolase superfamily. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present in the vicinity of a second, relatively unrelated enzyme (ortholog 1, TIGR03100) of the same superfamily.
Pssm-ID: 274428 Cd Length: 266 Bit Score: 38.26 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1851859573 69 IIFIPGYLSNMNGIKAVAV---EEFCKsLGHAFIRFDYSGIGSSDGNLAECTVGKWRKDVLSI---LDDVAEGPQILVGS 142
Cdd:TIGR03101 28 VIYLPPFAEEMNKSRRMVAlqaRAFAA-GGFGVLQIDLYGCGDSAGDFAAARWDVWKEDVAAAyrwLIEQGHPPVTLWGL 106
|
90 100
....*....|....*....|..
gi 1851859573 143 SLGGWLMLHAAIARPEKVIALI 164
Cdd:TIGR03101 107 RLGALLALDAANPLAAKCNRLV 128
|
|
|