|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
7-283 |
8.05e-44 |
|
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: 149.00 E-value: 8.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 7 TDGWIVSDGLRLHYVSWGrDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWdPRREYYAAAYVRDLD 86
Cdd:COG0596 3 TPRFVTVDGVRLHYREAG-PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 87 ALVRALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVIEDmgpgasvgsqgsarikrellETPDGFATWAdarvfwrrQ 166
Cdd:COG0596 81 ALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD--------------------EVLAALAEPL--------R 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 167 RPNLPEAALDSRVAHSLREhapgrivwrhdaagiaaarlaatpeqlvDLWPLIRSLRVPTLLLRGGDSDFLSAQVAADMS 246
Cdd:COG0596 133 RPGLAPEALAALLRALART----------------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
|
250 260 270
....*....|....*....|....*....|....*..
gi 981254954 247 AANAVIERVDIAGATHYVHDDRPAAFNGALREWLDRL 283
Cdd:COG0596 185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
29-269 |
1.46e-21 |
|
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: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 29 PAVVMLHGLRSYAQTWADVAHAL-TDRYRVVALDQRGRGASD-WDPRREYYAAAYVRDLDALVRALGLRRFVLVGHSMGG 106
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSrPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 107 ANAFVYAGRDPERLAGLViedmgpgaSVGSQGSARIKRELLETPD-GFATWADARVFWRRQRPNLPeaALDSRVAHSLRE 185
Cdd:pfam00561 81 LIALAYAAKYPDRVKALV--------LLGALDPPHELDEADRFILaLFPGFFDGFVADFAPNPLGR--LVAKLLALLLLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 186 HAPGRIV-------WRHDAAGIAAARLAATPEQLVDLW----PLIRSLRVPTLLLRGGDSDFLSAQVAADMSAANAVIER 254
Cdd:pfam00561 151 LRLLKALpllnkrfPSGDYALAKSLVTGALLFIETWSTelraKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230
|
250
....*....|....*
gi 981254954 255 VDIAGATHYVHDDRP 269
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
15-124 |
3.17e-15 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 74.26 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 15 GLRLHYVSWGrdDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDwDPRREYYAAAYVRDLDALVRALGL 94
Cdd:PRK03592 16 GSRMAYIETG--EGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASD-KPDIDYTFADHARYLDAWFDALGL 92
|
90 100 110
....*....|....*....|....*....|
gi 981254954 95 RRFVLVGHSMGGANAFVYAGRDPERLAGLV 124
Cdd:PRK03592 93 DDVVLVGHDWGSALGFDWAARHPDRVRGIA 122
|
|
| pro_imino_pep_1 |
TIGR01249 |
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ... |
12-125 |
2.71e-08 |
|
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.
Pssm-ID: 130316 [Multi-domain] Cd Length: 306 Bit Score: 54.07 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 12 VSDGLRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGasdwdpRREYYAAAY-------VRD 84
Cdd:TIGR01249 11 VSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCG------KSTPHACLEenttwdlVAD 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 981254954 85 LDALVRALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVI 125
Cdd:TIGR01249 85 IEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVL 125
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
41-161 |
9.78e-04 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 39.52 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 41 AQTWADVAHALTDRYRVVALDQRGRGASDWDPRREYYAAAYVrdLDALVRALGLRRFVLVGHSMGGANAFVYAGRDPER- 119
Cdd:smart00824 12 PHEYARLAAALRGRRDVSALPLPGFGPGEPLPASADALVEAQ--AEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARg 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 981254954 120 --LAGLVIEDMGPGASVGSQG-SARIKRELLETPDGFATWADARV 161
Cdd:smart00824 90 ipPAAVVLLDTYPPGDPAPEGwLPELLRGVFEREDSFVPMDDARL 134
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
98-130 |
6.28e-03 |
|
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: 37.59 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....
gi 981254954 98 VLVGHSMGGANAFVYAGRDPERLAGLV-IEDMGP 130
Cdd:cd12809 174 ILITHSQGGPFGWLAADARPDLVKAIVaIEPSGP 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
7-283 |
8.05e-44 |
|
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: 149.00 E-value: 8.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 7 TDGWIVSDGLRLHYVSWGrDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWdPRREYYAAAYVRDLD 86
Cdd:COG0596 3 TPRFVTVDGVRLHYREAG-PDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDK-PAGGYTLDDLADDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 87 ALVRALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVIEDmgpgasvgsqgsarikrellETPDGFATWAdarvfwrrQ 166
Cdd:COG0596 81 ALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD--------------------EVLAALAEPL--------R 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 167 RPNLPEAALDSRVAHSLREhapgrivwrhdaagiaaarlaatpeqlvDLWPLIRSLRVPTLLLRGGDSDFLSAQVAADMS 246
Cdd:COG0596 133 RPGLAPEALAALLRALART----------------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLA 184
|
250 260 270
....*....|....*....|....*....|....*..
gi 981254954 247 AANAVIERVDIAGATHYVHDDRPAAFNGALREWLDRL 283
Cdd:COG0596 185 ELLPNAELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1-169 |
1.52e-23 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 95.84 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 1 MNRASGTdgWIVSDGLRLHYVSWGRDDAP--AVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRREYY 77
Cdd:COG2267 1 MTRRLVT--LPTRDGLRLRGRRWRPAGSPrgTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRGHVDS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 78 AAAYVRDLDALVRALGLR---RFVLVGHSMGGANAFVYAGRDPERLAGLV------IEDMGPGASVGSQGSARIKREL-- 146
Cdd:COG2267 79 FDDYVDDLRAALDALRARpglPVVLLGHSMGGLIALLYAARYPDRVAGLVllapayRADPLLGPSARWLRALRLAEALar 158
|
170 180 190
....*....|....*....|....*....|.
gi 981254954 147 LETP--------DGFATWADARVFWRRQRPN 169
Cdd:COG2267 159 IDVPvlvlhggaDRVVPPEAARRLAARLSPD 189
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
29-269 |
1.46e-21 |
|
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: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 29 PAVVMLHGLRSYAQTWADVAHAL-TDRYRVVALDQRGRGASD-WDPRREYYAAAYVRDLDALVRALGLRRFVLVGHSMGG 106
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALaRDGFRVIALDLRGFGKSSrPKAQDDYRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 107 ANAFVYAGRDPERLAGLViedmgpgaSVGSQGSARIKRELLETPD-GFATWADARVFWRRQRPNLPeaALDSRVAHSLRE 185
Cdd:pfam00561 81 LIALAYAAKYPDRVKALV--------LLGALDPPHELDEADRFILaLFPGFFDGFVADFAPNPLGR--LVAKLLALLLLR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 186 HAPGRIV-------WRHDAAGIAAARLAATPEQLVDLW----PLIRSLRVPTLLLRGGDSDFLSAQVAADMSAANAVIER 254
Cdd:pfam00561 151 LRLLKALpllnkrfPSGDYALAKSLVTGALLFIETWSTelraKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARL 230
|
250
....*....|....*
gi 981254954 255 VDIAGATHYVHDDRP 269
Cdd:pfam00561 231 VVIPDAGHFAFLEGP 245
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
30-124 |
5.69e-17 |
|
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: 78.02 E-value: 5.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 30 AVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDwdPRREYYAA--AYVRDLDALVRAL-----GLRRFVLvG 101
Cdd:pfam12146 6 VVVLVHGLGEHSGRYAHLADALAAQgFAVYAYDHRGHGRSD--GKRGHVPSfdDYVDDLDTFVDKIreehpGLPLFLL-G 82
|
90 100
....*....|....*....|...
gi 981254954 102 HSMGGANAFVYAGRDPERLAGLV 124
Cdd:pfam12146 83 HSMGGLIAALYALRYPDKVDGLI 105
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
15-124 |
3.17e-15 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 74.26 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 15 GLRLHYVSWGrdDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDwDPRREYYAAAYVRDLDALVRALGL 94
Cdd:PRK03592 16 GSRMAYIETG--EGDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASD-KPDIDYTFADHARYLDAWFDALGL 92
|
90 100 110
....*....|....*....|....*....|
gi 981254954 95 RRFVLVGHSMGGANAFVYAGRDPERLAGLV 124
Cdd:PRK03592 93 DDVVLVGHDWGSALGFDWAARHPDRVRGIA 122
|
|
| PRK10673 |
PRK10673 |
esterase; |
27-281 |
2.43e-13 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 68.22 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 27 DAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWDPRREYYAAAyvRDLDALVRALGLRRFVLVGHSMGG 106
Cdd:PRK10673 15 NNSPIVLVHGLFGSLDNLGVLARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMA--QDLLDTLDALQIEKATFIGHSMGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 107 ANAFVYAGRDPERLAGLVIEDMGPgasVGSQgsARIKRELletpdgFATW---ADARVFWRRQ-----RPNLPEAALDSR 178
Cdd:PRK10673 93 KAVMALTALAPDRIDKLVAIDIAP---VDYH--VRRHDEI------FAAInavSEAGATTRQQaaaimRQHLNEEGVIQF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 179 VAHSLREHApgrivWRHDAAGIAAARLAATPEQLVDLWPlirslrVPTLLLRGGDSDFLSAQ----VAADMSAANAVIer 254
Cdd:PRK10673 162 LLKSFVDGE-----WRFNVPVLWDQYPHIVGWEKIPAWP------HPALFIRGGNSPYVTEAyrddLLAQFPQARAHV-- 228
|
250 260
....*....|....*....|....*..
gi 981254954 255 vdIAGATHYVHDDRPAAFNGALREWLD 281
Cdd:PRK10673 229 --IAGAGHWVHAEKPDAVLRAIRRYLN 253
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
7-124 |
1.24e-12 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 67.70 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 7 TDGWIVSDGLRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDW-DPRREYYAAAYVRDL 85
Cdd:PRK05855 4 RRTVVSSDGVRLAVYEWGDPDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSApKRTAAYTLARLADDF 83
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 981254954 86 DALVRALGLRRFV-LVGHSMGGANAFVYAGRdpERLAGLV 124
Cdd:PRK05855 84 AAVIDAVSPDRPVhLLAHDWGSIQGWEAVTR--PRAAGRI 121
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
10-278 |
3.18e-12 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 65.65 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 10 WIVSDGLRLHYVSWGrdDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWDPRREYYAAAYVRDLDALV 89
Cdd:PRK03204 18 WFDSSRGRIHYIDEG--TGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFGYQIDEHARVIGEFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 90 RALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVIEDMgpgasvgsqgsarikreLLETPDGFATWADARVFWRR--QR 167
Cdd:PRK03204 96 DHLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNT-----------------WFWPADTLAMKAFSRVMSSPpvQY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 168 PNLPEAALDSRVAHSLREHAPGRIVWRH----DAAGIAAARLAATPEQLVDLWPLIRSLR---------VPTLLLRG-GD 233
Cdd:PRK03204 159 AILRRNFFVERLIPAGTEHRPSSAVMAHyravQPNAAARRGVAEMPKQILAARPLLARLArevpatlgtKPTLLVWGmKD 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 981254954 234 SDFLSAQVAADMSAANAVIERVDIAGATHYVHDDRPAAFNGALRE 278
Cdd:PRK03204 239 VAFRPKTILPRLRATFPDHVLVELPNAKHFIQEDAPDRIAAAIIE 283
|
|
| PLN02578 |
PLN02578 |
hydrolase |
15-280 |
4.22e-12 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 65.63 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 15 GLRLHYVSWGRddAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDwDPRREYYAAAYVRDLDALVRALGL 94
Cdd:PLN02578 75 GHKIHYVVQGE--GLPIVLIHGFGASAFHWRYNIPELAKKYKVYALDLLGFGWSD-KALIEYDAMVWRDQVADFVKEVVK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 95 RRFVLVGHSMGGANAFVYAGRDPERLAGLVIedMGPGASVGSQGSARIKRELLETP-----------DGFATWADARVFW 163
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVAL--LNSAGQFGSESREKEEAIVVEETvltrfvvkplkEWFQRVVLGFLFW 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 164 RRQRPNLPEAAL----------DSRVAHSLREHA----PGRIVWRhdaagiaAARLAATPEQLVDLWPLIRSLRVPTLLL 229
Cdd:PLN02578 230 QAKQPSRIESVLksvykdksnvDDYLVESITEPAadpnAGEVYYR-------LMSRFLFNQSRYTLDSLLSKLSCPLLLL 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981254954 230 rGGDSDFLSAQVAADMSAA---NAVIERVDiagATHYVHDDRPAAFNGALREWL 280
Cdd:PLN02578 303 -WGDLDPWVGPAKAEKIKAfypDTTLVNLQ---AGHCPHDEVPEQVNKALLEWL 352
|
|
| FrsA |
COG1073 |
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ... |
13-282 |
5.25e-12 |
|
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms];
Pssm-ID: 440691 [Multi-domain] Cd Length: 253 Bit Score: 64.55 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 13 SDGLRLH---YV-SWGRDDAPAVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRreYYAAAYVRDLDA 87
Cdd:COG1073 18 RDGIKLAgdlYLpAGASKKYPAVVVAHGNGGVKEQRALYAQRLAELgFNVLAFDYRGYGESEGEPR--EEGSPERRDARA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 88 LVRALGLRRFV------LVGHSMGGANAFVYAGRDPeRLAGLVIEdmGPGASVGSQGSARikrelletpdgfatWADARV 161
Cdd:COG1073 96 AVDYLRTLPGVdperigLLGISLGGGYALNAAATDP-RVKAVILD--SPFTSLEDLAAQR--------------AKEARG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 162 FWRRQRPNLPEAALDSRVahslrehapgrivwrhdaagiaaarlaatpEQLVDLWPLIRSLRVPTLLLRGGDSDFlsaqV 241
Cdd:COG1073 159 AYLPGVPYLPNVRLASLL------------------------------NDEFDPLAKIEKISRPLLFIHGEKDEA----V 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 981254954 242 AADMS-----AANAVIERVDIAGATHY-VHDDRPAAFNGALREWLDR 282
Cdd:COG1073 205 PFYMSedlyeAAAEPKELLIVPGAGHVdLYDRPEEEYFDKLAEFFKK 251
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
14-278 |
1.88e-11 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 63.81 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 14 DGLRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWDPRR---EYYAAAYVRDLDALvr 90
Cdd:PRK14875 117 GGRTVRYLRLGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGASSKAVGAgslDELAAAVLAFLDAL-- 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 91 alGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVIedMGPgASVGSQgsarIKRELLetpDGFATwADARvfwRRQRPNL 170
Cdd:PRK14875 195 --GIERAHLVGHSMGGAVALRLAARAPQRVASLTL--IAP-AGLGPE----INGDYI---DGFVA-AESR---RELKPVL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 171 PE----AALDSR--VAHSLREHapgRIVWRHDAAGIAAARLAATPEQLVDLWPLIRSLRVPTLLLRGGDSDFLSAQVAAD 244
Cdd:PRK14875 259 ELlfadPALVTRqmVEDLLKYK---RLDGVDDALRALADALFAGGRQRVDLRDRLASLAIPVLVIWGEQDRIIPAAHAQG 335
|
250 260 270
....*....|....*....|....*....|....
gi 981254954 245 MsAANAVIERVDIAGatHYVHDDRPAAFNGALRE 278
Cdd:PRK14875 336 L-PDGVAVHVLPGAG--HMPQMEAAADVNRLLAE 366
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
24-276 |
3.91e-11 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 63.01 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 24 GRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASDWDP----RREYYAAAYVRDLDALVRALGLRRFVL 99
Cdd:PLN02894 101 SKEDAPTLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPDftckSTEETEAWFIDSFEEWRKAKNLSNFIL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 100 VGHSMGGANAFVYAGRDPERLAGLVIedMGP-GASVGSQGSAR------------IKRELLE---TPD----GFATW--- 156
Cdd:PLN02894 181 LGHSFGGYVAAKYALKHPEHVQHLIL--VGPaGFSSESDDKSEwltkfratwkgaVLNHLWEsnfTPQkiirGLGPWgpn 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 157 -----ADARVFWRRQRPNLPEAA---LDSRVAHSLREHAPGRIVWRHDAAGIAAARLaatpeqlvdlwPLIRSL---RVP 225
Cdd:PLN02894 259 lvrryTTARFGAHSTGDILSEEEsklLTDYVYHTLAAKASGELCLKYIFSFGAFARK-----------PLLESAsewKVP 327
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 981254954 226 TLLLRGGDsDFLSAQVAADMSAANAV---IERVDIAGatHYVHDDRPAAFNGAL 276
Cdd:PLN02894 328 TTFIYGRH-DWMNYEGAVEARKRMKVpceIIRVPQGG--HFVFLDNPSGFHSAV 378
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
13-124 |
7.40e-11 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 60.80 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 13 SDGLRLH---YVSWGRDDAPAVVMLHGL-RSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRREYyaaayVRDLDA 87
Cdd:COG1506 5 ADGTTLPgwlYLPADGKKYPVVVYVHGGpGSRDDSFLPLAQALASRgYAVLAPDYRGYGESAGDWGGDE-----VDDVLA 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 981254954 88 LVRAL------GLRRFVLVGHSMGGANAFVYAGRDPERLAGLV 124
Cdd:COG1506 80 AIDYLaarpyvDPDRIGIYGHSYGGYMALLAAARHPDRFKAAV 122
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
31-124 |
8.48e-11 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 57.92 E-value: 8.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 31 VVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDprreyyAAAYVRD-LDALVRALGLRRFVLVGHSMGG-- 106
Cdd:COG1075 8 VVLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGSIED------SAEQLAAfVDAVLAATGAEKVDLVGHSMGGlv 81
|
90
....*....|....*...
gi 981254954 107 ANAFVYAGRDPERLAGLV 124
Cdd:COG1075 82 ARYYLKRLGGAAKVARVV 99
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
16-175 |
2.68e-10 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 59.98 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 16 LRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRREYYA-AAYVRDLDALVRALG 93
Cdd:PRK00870 34 LRMHYVDEGPADGPPVLLLHGEPSWSYLYRKMIPILAAAgHRVIAPDLIGFGRSDKPTRREDYTyARHVEWMRSWFEQLD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 94 LRRFVLVGHSMGGANAFVYAGRDPERLAGLVIedMGPGASVGSQgsarikrellETPDGFATWADArvfwRRQRPNLPEA 173
Cdd:PRK00870 114 LTDVTLVCQDWGGLIGLRLAAEHPDRFARLVV--ANTGLPTGDG----------PMPDAFWAWRAF----SQYSPVLPVG 177
|
..
gi 981254954 174 AL 175
Cdd:PRK00870 178 RL 179
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
31-275 |
2.10e-08 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 53.63 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 31 VVMLHGLrsyAQTWADVAHALTDRYRVVALDQRGRGASDwdprREYYAAAYVRDLDALVRALG-LRRFVLVGHSMGGANA 109
Cdd:pfam12697 1 VVLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSS----PPPLDLADLADLAALLDELGaARPVVLVGHSLGGAVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 110 fvYAGRDPERLAGLVIEDMGPGASVGsqgsarikrelletpdgfatwADARVFWRRQRPNLPEAALDSRVahSLREHAPG 189
Cdd:pfam12697 74 --LAAAAAALVVGVLVAPLAAPPGLL---------------------AALLALLARLGAALAAPAWLAAE--SLARGFLD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 190 RIVWRHDAAGIAAARLAATPEQLVDLWPLIRSLRVPTLLLrgGDSDFLSAQVAADMSAANAVIERVDIAGATHYVHDDrP 269
Cdd:pfam12697 129 DLPADAEWAAALARLAALLAALALLPLAAWRDLPVPVLVL--AEEDRLVPELAQRLLAALAGARLVVLPGAGHLPLDD-P 205
|
....*.
gi 981254954 270 AAFNGA 275
Cdd:pfam12697 206 EEVAEA 211
|
|
| pro_imino_pep_1 |
TIGR01249 |
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related ... |
12-125 |
2.71e-08 |
|
proline iminopeptidase, Neisseria-type subfamily; This model represents one of two related families of proline iminopeptidase in the alpha/beta fold hydrolase family. The fine specificities of the various members, including both the range of short peptides from which proline can be removed and whether other amino acids such as alanine can be also removed, may vary among members.
Pssm-ID: 130316 [Multi-domain] Cd Length: 306 Bit Score: 54.07 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 12 VSDGLRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGasdwdpRREYYAAAY-------VRD 84
Cdd:TIGR01249 11 VSDNHQLYYEQSGNPDGKPVVFLHGGPGSGTDPGCRRFFDPETYRIVLFDQRGCG------KSTPHACLEenttwdlVAD 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 981254954 85 LDALVRALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVI 125
Cdd:TIGR01249 85 IEKLREKLGIKNWLVFGGSWGSTLALAYAQTHPEVVTGLVL 125
|
|
| PLN03084 |
PLN03084 |
alpha/beta hydrolase fold protein; Provisional |
6-125 |
3.00e-08 |
|
alpha/beta hydrolase fold protein; Provisional
Pssm-ID: 178633 Cd Length: 383 Bit Score: 54.12 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 6 GTDGWIVSDGLRLHYVSWGRDDAPAVVMLHGLRSYAQTWADVAHALTDRYRVVALDQRGRGASD---WDPRREYYAAAYV 82
Cdd:PLN03084 105 GAQSQASSDLFRWFCVESGSNNNPPVLLIHGFPSQAYSYRKVLPVLSKNYHAIAFDWLGFGFSDkpqPGYGFNYTLDEYV 184
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 981254954 83 RDLDALVRALGLRRFVLVGHSMGGANAFVYAGRDPERLAGLVI 125
Cdd:PLN03084 185 SSLESLIDELKSDKVSLVVQGYFSPPVVKYASAHPDKIKKLIL 227
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
27-131 |
1.57e-07 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 51.38 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 27 DAPAVVMLHGLRSYAQTWADVAHALTDrYRVVALDQRGRGAS------DWDPRREYyaaayvrdLDALVRALGLRRFVLV 100
Cdd:PRK11126 1 GLPWLVFLHGLLGSGQDWQPVGEALPD-YPRLYIDLPGHGGSaaisvdGFADVSRL--------LSQTLQSYNILPYWLV 71
|
90 100 110
....*....|....*....|....*....|..
gi 981254954 101 GHSMGGANAFVYA-GRDPERLAGLVIEDMGPG 131
Cdd:PRK11126 72 GYSLGGRIAMYYAcQGLAGGLCGLIVEGGNPG 103
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
28-147 |
2.02e-07 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 50.74 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 28 APAVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRR------EYYAAAYVRDLDALVRALGLR----- 95
Cdd:COG0412 29 RPGVVVLHEIFGLNPHIRDVARRLAAAgYVVLAPDLYGRGGPGDDPDEaralmgALDPELLAADLRAALDWLKAQpevda 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 981254954 96 -RFVLVGHSMGGANAFVYAGRDPeRLAGLVIEDMGPGASVGSQGSARIKRELL 147
Cdd:COG0412 109 gRVGVVGFCFGGGLALLAAARGP-DLAAAVSFYGGLPADDLLDLAARIKAPVL 160
|
|
| YheT |
COG0429 |
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only]; |
10-123 |
6.30e-07 |
|
Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only];
Pssm-ID: 440198 [Multi-domain] Cd Length: 323 Bit Score: 49.76 E-value: 6.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 10 WIVSDG--LRLHYVSWGRDDAPAVVMLHGL-----RSYAQTWADVAHALtdRYRVVALDQRGRGASDWDPRREYYAAAyV 82
Cdd:COG0429 41 LELPDGdfVDLDWSDPPAPSKPLVVLLHGLegssdSHYARGLARALYAR--GWDVVRLNFRGCGGEPNLLPRLYHSGD-T 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 981254954 83 RDLDALVRAL----GLRRFVLVGHSMGGaNAFV-YAGRDPERLAGL 123
Cdd:COG0429 118 EDLVWVLAHLraryPYAPLYAVGFSLGG-NLLLkYLGEQGDDAPPL 162
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
24-124 |
4.26e-06 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 46.44 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 24 GRDDAPAVVMLHGLRSYAQTWADVAHAL-TDRYRVVAL------DQRGR-------GASDWDPRREYYAAAYVRD-LDAL 88
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLLPLAPELaLPGAAVLAPrapvpeGPGGRawfdlsfLEGREDEEGLAAAAEALAAfIDEL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 981254954 89 VRALGL--RRFVLVGHSMGGANAFVYAGRDPERLAGLV 124
Cdd:COG0400 81 EARYGIdpERIVLAGFSQGAAMALSLALRRPELLAGVV 118
|
|
| FrmB |
COG0627 |
S-formylglutathione hydrolase FrmB [Defense mechanisms]; |
22-119 |
4.94e-05 |
|
S-formylglutathione hydrolase FrmB [Defense mechanisms];
Pssm-ID: 440392 [Multi-domain] Cd Length: 249 Bit Score: 43.67 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 22 SWGRDDAPAVVMLHGLRSYAQTWADVAHA--LTDRYR--VVALDQRGRGA-SDW--DPRREYYAAAYV-RDLDALVRA-L 92
Cdd:COG0627 27 GYDGRPLPVLYLLHGLTGTHENWTRKTGAqrLAAELGviVVMPDGGQASFyVDWtqGPAGHYRWETYLtEELPPLIEAnF 106
|
90 100 110
....*....|....*....|....*....|..
gi 981254954 93 GL-----RRFVlVGHSMGGANAFVYAGRDPER 119
Cdd:COG0627 107 PVsadreRRAI-AGLSMGGHGALTLALRHPDL 137
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
29-124 |
5.95e-04 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 40.31 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 29 PAVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRReYYAAAYVRDLDALVRAL--GLRRFVLVGHSMG 105
Cdd:COG1647 16 KGVLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSPEDLLK-TTWEDWLEDVEEAYEILkaGYDKVIVIGLSMG 94
|
90
....*....|....*....
gi 981254954 106 GANAFVYAGRDPErLAGLV 124
Cdd:COG1647 95 GLLALLLAARYPD-VAGLV 112
|
|
| LpqC |
COG3509 |
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and ... |
28-125 |
8.01e-04 |
|
Acetyl xylan esterase AxeA and related esterases, LpqC family [Carbohydrate transport and metabolism];
Pssm-ID: 442732 [Multi-domain] Cd Length: 284 Bit Score: 40.37 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 28 APAVVMLHGlrsYAQTWADVA-----HALTDRYR--VVALDQRGRGAS----DWDPRREYYAAAYVRDLDALVRALGLR- 95
Cdd:COG3509 53 LPLVVALHG---CGGSAADFAagtglNALADREGfiVVYPEGTGRAPGrcwnWFDGRDQRRGRDDVAFIAALVDDLAARy 129
|
90 100 110
....*....|....*....|....*....|....*
gi 981254954 96 -----RFVLVGHSMGGANAFVYAGRDPERLAGLVI 125
Cdd:COG3509 130 gidpkRVYVTGLSAGGAMAYRLACEYPDVFAAVAP 164
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
41-161 |
9.78e-04 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 39.52 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 41 AQTWADVAHALTDRYRVVALDQRGRGASDWDPRREYYAAAYVrdLDALVRALGLRRFVLVGHSMGGANAFVYAGRDPER- 119
Cdd:smart00824 12 PHEYARLAAALRGRRDVSALPLPGFGPGEPLPASADALVEAQ--AEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARg 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 981254954 120 --LAGLVIEDMGPGASVGSQG-SARIKRELLETPDGFATWADARV 161
Cdd:smart00824 90 ipPAAVVLLDTYPPGDPAPEGwLPELLRGVFEREDSFVPMDDARL 134
|
|
| COG4188 |
COG4188 |
Predicted dienelactone hydrolase [General function prediction only]; |
29-114 |
4.38e-03 |
|
Predicted dienelactone hydrolase [General function prediction only];
Pssm-ID: 443342 [Multi-domain] Cd Length: 326 Bit Score: 38.16 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981254954 29 PAVVMLHGLRSYAQTWADVAHALTDR-YRVVALDQRGRGASDWDPRREYYAAAY--------VRD----LDALVR----- 90
Cdd:COG4188 63 PLVVLSHGLGGSREGYAYLAEHLASHgYVVAAPDHPGSNAADLSAALDGLADALdpeelwerPLDlsfvLDQLLAlnksd 142
|
90 100
....*....|....*....|....*....
gi 981254954 91 -----ALGLRRFVLVGHSMGGANAFVYAG 114
Cdd:COG4188 143 pplagRLDLDRIGVIGHSLGGYTALALAG 171
|
|
| Esterase_713_like-2 |
cd12809 |
Uncharacterized enzymes similar to novel bacterial esterase that cleaves esters on halogenated ... |
98-130 |
6.28e-03 |
|
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: 37.59 E-value: 6.28e-03
10 20 30
....*....|....*....|....*....|....
gi 981254954 98 VLVGHSMGGANAFVYAGRDPERLAGLV-IEDMGP 130
Cdd:cd12809 174 ILITHSQGGPFGWLAADARPDLVKAIVaIEPSGP 207
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
72-125 |
9.11e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 36.87 E-value: 9.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981254954 72 PRREYYAAA-YVRDLDALVRALGLRRFV------LVGHSMGGANAFVYAGRDPERLAGLVI 125
Cdd:COG4099 95 PEDDYWSDTkALDAVLALLDDLIAEYRIdpdriyLTGLSMGGYGTWDLAARYPDLFAAAVP 155
|
|
| |
