|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
4-260 |
1.62e-35 |
|
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: 126.27 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYSTLG-EGYPIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKP-RHIEIKDFSDDIVELLKY 81
Cdd:COG0596 6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAALLDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 82 LYIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNPTsiegelpeerlfrkYAHIIRNWdpekqdkflnKRKYYRPRKM 161
Cdd:COG0596 86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV--------------LAALAEPL----------RRPGLAPEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 162 NRFLKHVVDTneistkeeiqavkevfknaDISQTYRNVVVPTKIIAGEFGERTTRLEAKEVADLIQNADFEVYQESSAFP 241
Cdd:COG0596 142 AALLRALART-------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
|
250
....*....|....*....
gi 593416183 242 FVEEQERFVEDTASFINKH 260
Cdd:COG0596 203 PLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
21-245 |
5.79e-17 |
|
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: 77.93 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 21 YPIVLIHTVLDNYSVFNKLAAQLAKS-FQVVLIDLRGHGYSDKPRHI---EIKDFSDDIVELLKYLYIEEVAFVCHEMGG 96
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQddyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 97 IIGADISVRYPEFTSSLMLVNPTSIEGELPEERLFrkyahiIRNWDPEKQDKFLNK----------------------RK 154
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRF------ILALFPGFFDGFVADfapnplgrlvakllallllrlrLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 155 YYRPRKMNRFLKHVVDtNEISTKEEIQAVKEVFKNADISQTYRNVVVPTKIIAGEfGERTTRLEAKEV-ADLIQNADFEV 233
Cdd:pfam00561 155 KALPLLNKRFPSGDYA-LAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGD-QDPLVPPQALEKlAQLFPNARLVV 232
|
250
....*....|..
gi 593416183 234 YQESSAFPFVEE 245
Cdd:pfam00561 233 IPDAGHFAFLEG 244
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-118 |
5.49e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 64.97 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYSTLGEGY--PIVLIHTV---LDNYsVFNKlaAQLAKSFQVVLIDLRGHGYSDKprHIE---IKDFSDDI 75
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDgtPVVLIHGFggdLNNW-LFNH--AALAAGRPVIALDLPGHGASSK--AVGagsLDELAAAV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 593416183 76 VELLKYLYIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNP 118
Cdd:PRK14875 188 LAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
18-257 |
7.91e-09 |
|
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: 54.82 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 18 GEGYP-IVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPRHIEIKDFSDDIVELLKYLYIeevaFVCHEMGG 96
Cdd:TIGR01738 1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAI----WLGWSLGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 97 IIGADISVRYPEFTSSLMLVNPT---SIEGELPE---ERLFRKYAHIIRNWDPEKQDKFLNKRKYYRP--RKMNRFLKHV 168
Cdd:TIGR01738 77 LVALHIAATHPDRVRALVTVASSpcfSAREDWPEgikPDVLTGFQQQLSDDYQRTIERFLALQTLGTPtaRQDARALKQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 169 VDTNEISTKEEIQAVKEVFKNADISQTYRNVVVPTKIIAGEFGERTTRLEAKEVADLIQNADFEVYQESSAFPFVEEQER 248
Cdd:TIGR01738 157 LLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEA 236
|
....*....
gi 593416183 249 FVEDTASFI 257
Cdd:TIGR01738 237 FCALLVAFK 245
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
4-260 |
1.62e-35 |
|
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: 126.27 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYSTLG-EGYPIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKP-RHIEIKDFSDDIVELLKY 81
Cdd:COG0596 6 FVTVDGVRLHYREAGpDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPaGGYTLDDLADDLAALLDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 82 LYIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNPTsiegelpeerlfrkYAHIIRNWdpekqdkflnKRKYYRPRKM 161
Cdd:COG0596 86 LGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEV--------------LAALAEPL----------RRPGLAPEAL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 162 NRFLKHVVDTneistkeeiqavkevfknaDISQTYRNVVVPTKIIAGEFGERTTRLEAKEVADLIQNADFEVYQESSAFP 241
Cdd:COG0596 142 AALLRALART-------------------DLRERLARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGAGHFP 202
|
250
....*....|....*....
gi 593416183 242 FVEEQERFVEDTASFINKH 260
Cdd:COG0596 203 PLEQPEAFAAALRDFLARL 221
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
21-245 |
5.79e-17 |
|
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: 77.93 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 21 YPIVLIHTVLDNYSVFNKLAAQLAKS-FQVVLIDLRGHGYSDKPRHI---EIKDFSDDIVELLKYLYIEEVAFVCHEMGG 96
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQddyRTDDLAEDLEYILEALGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 97 IIGADISVRYPEFTSSLMLVNPTSIEGELPEERLFrkyahiIRNWDPEKQDKFLNK----------------------RK 154
Cdd:pfam00561 81 LIALAYAAKYPDRVKALVLLGALDPPHELDEADRF------ILALFPGFFDGFVADfapnplgrlvakllallllrlrLL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 155 YYRPRKMNRFLKHVVDtNEISTKEEIQAVKEVFKNADISQTYRNVVVPTKIIAGEfGERTTRLEAKEV-ADLIQNADFEV 233
Cdd:pfam00561 155 KALPLLNKRFPSGDYA-LAKSLVTGALLFIETWSTELRAKFLGRLDEPTLIIWGD-QDPLVPPQALEKlAQLFPNARLVV 232
|
250
....*....|..
gi 593416183 234 YQESSAFPFVEE 245
Cdd:pfam00561 233 IPDAGHFAFLEG 244
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
4-118 |
5.49e-12 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 64.97 E-value: 5.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYSTLGEGY--PIVLIHTV---LDNYsVFNKlaAQLAKSFQVVLIDLRGHGYSDKprHIE---IKDFSDDI 75
Cdd:PRK14875 113 KARIGGRTVRYLRLGEGDgtPVVLIHGFggdLNNW-LFNH--AALAAGRPVIALDLPGHGASSK--AVGagsLDELAAAV 187
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 593416183 76 VELLKYLYIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNP 118
Cdd:PRK14875 188 LAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLIAP 230
|
|
| PLN02824 |
PLN02824 |
hydrolase, alpha/beta fold family protein |
9-119 |
5.97e-12 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 178419 [Multi-domain] Cd Length: 294 Bit Score: 64.37 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 9 GTSIHYSTLG-EGYPIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPRHIE---------------IKDFS 72
Cdd:PLN02824 17 GYNIRYQRAGtSGPALVLVHGFGGNADHWRKNTPVLAKSHRVYAIDLLGYGYSDKPNPRSappnsfytfetwgeqLNDFC 96
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 593416183 73 DDIVEllkylyiEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNPT 119
Cdd:PLN02824 97 SDVVG-------DPAFVICNSVGGVVGLQAAVDAPELVRGVMLINIS 136
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
4-125 |
1.59e-11 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 62.33 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYSTL----GEGYPIVLIHTVLDNYSVFNKLAAQLAKS-FQVVLIDLRGHGYSDKPR-HIE-IKDFSDDIV 76
Cdd:COG2267 8 LPTRDGLRLRGRRWrpagSPRGTVVLVHGLGEHSGRYAELAEALAAAgYAVLAFDLRGHGRSDGPRgHVDsFDDYVDDLR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 593416183 77 ELLKYL---YIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNPTSIEGEL 125
Cdd:COG2267 88 AALDALrarPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPAYRADPL 139
|
|
| PRK10673 |
PRK10673 |
esterase; |
22-117 |
2.30e-11 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 62.05 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 22 PIVLIHTV---LDNYSVfnkLAAQLAKSFQVVLIDLRGHGYSDKPRHIEIKDFSDDIVELLKYLYIEEVAFVCHEMGGII 98
Cdd:PRK10673 18 PIVLVHGLfgsLDNLGV---LARDLVNDHDIIQVDMRNHGLSPRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKA 94
|
90
....*....|....*....
gi 593416183 99 GADISVRYPEFTSSLMLVN 117
Cdd:PRK10673 95 VMALTALAPDRIDKLVAID 113
|
|
| PLN02578 |
PLN02578 |
hydrolase |
9-141 |
2.41e-11 |
|
hydrolase
Pssm-ID: 215315 [Multi-domain] Cd Length: 354 Bit Score: 62.94 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 9 GTSIHYSTLGEGYPIVLIHTVldNYSVFNKL--AAQLAKSFQVVLIDLRGHGYSDKPRhIEIKDF--SDDIVELLKYLYI 84
Cdd:PLN02578 75 GHKIHYVVQGEGLPIVLIHGF--GASAFHWRynIPELAKKYKVYALDLLGFGWSDKAL-IEYDAMvwRDQVADFVKEVVK 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 593416183 85 EEVAFVCHEMGGIIGADISVRYPEFTSSLMLVNPT---------SIEGELPEERLFRKYA-HIIRNW 141
Cdd:PLN02578 152 EPAVLVGNSLGGFTALSTAVGYPELVAGVALLNSAgqfgsesreKEEAIVVEETVLTRFVvKPLKEW 218
|
|
| Hydrolase_4 |
pfam12146 |
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ... |
23-209 |
7.31e-11 |
|
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: 60.69 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 23 IVLIHTVLDNYSVFNKLAAQLAK-SFQVVLIDLRGHGYSDKPR-HIE-IKDFSDDIVELLKYLYIEE----VAFVCHEMG 95
Cdd:pfam12146 7 VVLVHGLGEHSGRYAHLADALAAqGFAVYAYDHRGHGRSDGKRgHVPsFDDYVDDLDTFVDKIREEHpglpLFLLGHSMG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 96 GIIGADISVRYPEFTSSLMLVNPtSIEGELPEERLFRKYAHIIRNW------------------DPEKQDKFLNKrKYYR 157
Cdd:pfam12146 87 GLIAALYALRYPDKVDGLILSAP-ALKIKPYLAPPILKLLAKLLGKlfprlrvpnnllpdslsrDPEVVAAYAAD-PLVH 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 593416183 158 PRKMNRFLKHVVDtneistkeeiqAVKEVFKNADisqtyrNVVVPTKIIAGE 209
Cdd:pfam12146 165 GGISARTLYELLD-----------AGERLLRRAA------AITVPLLLLHGG 199
|
|
| PRK05855 |
PRK05855 |
SDR family oxidoreductase; |
3-64 |
3.85e-09 |
|
SDR family oxidoreductase;
Pssm-ID: 235628 [Multi-domain] Cd Length: 582 Bit Score: 56.91 E-value: 3.85e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 593416183 3 LFTRKDGTSIHYSTLG--EGYPIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPR 64
Cdd:PRK05855 6 TVVSSDGVRLAVYEWGdpDRPTVVLVHGYPDNHEVWDGVAPLLADRFRVVAYDVRGAGRSSAPK 69
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
18-257 |
7.91e-09 |
|
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: 54.82 E-value: 7.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 18 GEGYP-IVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPRHIEIKDFSDDIVELLKYLYIeevaFVCHEMGG 96
Cdd:TIGR01738 1 GQGNVhLVLIHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFGPLSLADMAEAIAAQAPDPAI----WLGWSLGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 97 IIGADISVRYPEFTSSLMLVNPT---SIEGELPE---ERLFRKYAHIIRNWDPEKQDKFLNKRKYYRP--RKMNRFLKHV 168
Cdd:TIGR01738 77 LVALHIAATHPDRVRALVTVASSpcfSAREDWPEgikPDVLTGFQQQLSDDYQRTIERFLALQTLGTPtaRQDARALKQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 169 VDTNEISTKEEIQAVKEVFKNADISQTYRNVVVPTKIIAGEFGERTTRLEAKEVADLIQNADFEVYQESSAFPFVEEQER 248
Cdd:TIGR01738 157 LLARPTPNVQVLQAGLEILATVDLRQPLQNISVPFLRLYGYLDGLVPAKVVPMLDKLAPHSELYIFAKAAHAPFLSHAEA 236
|
....*....
gi 593416183 249 FVEDTASFI 257
Cdd:TIGR01738 237 FCALLVAFK 245
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
23-251 |
8.98e-09 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 54.40 E-value: 8.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 23 IVLIHtvlDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPRHieikDFSD--DIVELLKYL-YIEEVAFVCHEMGGIIG 99
Cdd:pfam12697 1 VVLVH---GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPL----DLADlaDLAALLDELgAARPVVLVGHSLGGAVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 100 ADISVRYPEFTsslMLVNPTSiegeLPEERLFRKYAHIIRNWDPEKQDKFLNKRKYYRprkmnRFLKHVVDTNEISTKEE 179
Cdd:pfam12697 74 LAAAAAALVVG---VLVAPLA----APPGLLAALLALLARLGAALAAPAWLAAESLAR-----GFLDDLPADAEWAAALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 593416183 180 IQAVKEVFKNADISQTYRNVVVPTKIIAGEfgERTTRLEAKEVADLIQNADFEVYQESSAFPFvEEQERFVE 251
Cdd:pfam12697 142 RLAALLAALALLPLAAWRDLPVPVLVLAEE--DRLVPELAQRLLAALAGARLVVLPGAGHLPL-DDPEEVAE 210
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
21-106 |
2.74e-07 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 47.90 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 21 YPIVLIHTVLDNYSVFNKLAAQLAKS-FQVVLIDlrghgYSDKPRHIEI--KDFSDDIVELLKYLYIEEVAFVCHEMGGI 97
Cdd:COG1075 6 YPVVLVHGLGGSAASWAPLAPRLRAAgYPVYALN-----YPSTNGSIEDsaEQLAAFVDAVLAATGAEKVDLVGHSMGGL 80
|
....*....
gi 593416183 98 IgadisVRY 106
Cdd:COG1075 81 V-----ARY 84
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
23-260 |
2.87e-06 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 47.24 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 23 IVLIHTVLDNYSVFNKLAAQLAKS-FQVVLIDLRGHGYS-DKPRHIEIKDFSDDIVELLKYL--YIEEVAFVCHEMGGII 98
Cdd:COG1647 18 VLLLHGFTGSPAEMRPLAEALAKAgYTVYAPRLPGHGTSpEDLLKTTWEDWLEDVEEAYEILkaGYDKVIVIGLSMGGLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 99 GADISVRYPEFtSSLMLVNPT-SIEGE-LPEERLFRKYAHIIRNWDPEKQDKFLNKRKYYR-P----RKMNRFLKHVvdt 171
Cdd:COG1647 98 ALLLAARYPDV-AGLVLLSPAlKIDDPsAPLLPLLKYLARSLRGIGSDIEDPEVAEYAYDRtPlralAELQRLIREV--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 172 neistKEEIQAVKevfknadisqtyrnvvVPTKIIAGEfGERTTRLE-AKEVADLIQNADFE--VYQESS-AFPFVEEQE 247
Cdd:COG1647 174 -----RRDLPKIT----------------APTLIIQSR-KDEVVPPEsARYIYERLGSPDKElvWLEDSGhVITLDKDRE 231
|
250
....*....|...
gi 593416183 248 RFVEDTASFINKH 260
Cdd:COG1647 232 EVAEEILDFLERL 244
|
|
| PLN02894 |
PLN02894 |
hydrolase, alpha/beta fold family protein |
22-132 |
5.76e-05 |
|
hydrolase, alpha/beta fold family protein
Pssm-ID: 215484 [Multi-domain] Cd Length: 402 Bit Score: 43.75 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 22 PIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKP----RHIEIKD--FSDDIVELLKYLYIEEVAFVCHEMG 95
Cdd:PLN02894 107 TLVMVHGYGASQGFFFRNFDALASRFRVIAIDQLGWGGSSRPdftcKSTEETEawFIDSFEEWRKAKNLSNFILLGHSFG 186
|
90 100 110
....*....|....*....|....*....|....*....
gi 593416183 96 GIIGADISVRYPEFTSSLMLVNPT--SIEGELPEERLFR 132
Cdd:PLN02894 187 GYVAAKYALKHPEHVQHLILVGPAgfSSESDDKSEWLTK 225
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
9-133 |
5.78e-05 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 43.44 E-value: 5.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 9 GTSIHYSTLGEGYPIVLIH---TvlDNYSVFNKLAAqLAKSFQVVLIDLRGHGYSDKP----RHIEIKDFSDDIVELLKy 81
Cdd:PRK03592 16 GSRMAYIETGEGDPIVFLHgnpT--SSYLWRNIIPH-LAGLGRCLAPDLIGMGASDKPdidyTFADHARYLDAWFDALG- 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 593416183 82 lyIEEVAFVCHEMGGIIGADISVRYPEFTSSLM----LVNPTSIEgELPEE--RLFRK 133
Cdd:PRK03592 92 --LDDVVLVGHDWGSALGFDWAARHPDRVRGIAfmeaIVRPMTWD-DFPPAvrELFQA 146
|
|
| PRK00870 |
PRK00870 |
haloalkane dehalogenase; Provisional |
12-135 |
3.38e-04 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179147 [Multi-domain] Cd Length: 302 Bit Score: 41.11 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 12 IHYSTLG--EGYPIVLIH-----TVLdnysvFNKLAAQLAKS-FQVVLIDLRGHGYSDKPRHIEikDFS-----DDIVEL 78
Cdd:PRK00870 36 MHYVDEGpaDGPPVLLLHgepswSYL-----YRKMIPILAAAgHRVIAPDLIGFGRSDKPTRRE--DYTyarhvEWMRSW 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 593416183 79 LKYLYIEEVAFVCHEMGGIIGADISVRYPEFTSSLMLVN---PTSiEGELPEE-RLFRKYA 135
Cdd:PRK00870 109 FEQLDLTDVTLVCQDWGGLIGLRLAAEHPDRFARLVVANtglPTG-DGPMPDAfWAWRAFS 168
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
4-109 |
1.44e-03 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 38.84 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 4 FTRKDGTSIHYsTL-----GEGYP-IVLIH---TVLDNYsvFNKLAAQLAKS-FQVVLIDLRGHGYSDkpRHIEIKDFsD 73
Cdd:COG1506 2 FKSADGTTLPG-WLylpadGKKYPvVVYVHggpGSRDDS--FLPLAQALASRgYAVLAPDYRGYGESA--GDWGGDEV-D 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 593416183 74 DIVELLKYL----YI--EEVAFVCHEMGGIIGADISVRYPEF 109
Cdd:COG1506 76 DVLAAIDYLaarpYVdpDRIGIYGHSYGGYMALLAAARHPDR 117
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
12-117 |
1.60e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 39.07 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593416183 12 IHYSTLGEGYPIVLIHTVLDNYSVFNKLAAQLAKSFQVVLIDLRGHGYSDKPRHI--EIKDFSDDIVELLKYLYIEEVAF 89
Cdd:PRK03204 26 IHYIDEGTGPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFGLSERPSGFgyQIDEHARVIGEFVDHLGLDRYLS 105
|
90 100
....*....|....*....|....*...
gi 593416183 90 VCHEMGGIIGADISVRYPEFTSSLMLVN 117
Cdd:PRK03204 106 MGQDWGGPISMAVAVERADRVRGVVLGN 133
|
|
| LETM1_RBD |
pfam07766 |
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a ... |
141-189 |
4.62e-03 |
|
LETM1-like, RBD; Members of this entry are inner mitochondrial membrane proteins which play a role in potassium and hydrogen ion exchange. Deletion of LETM1 is thought to be involved in the development of Wolf-Hirschhorn syndrome in humans. This entry represents the ribosome-binding domain (RBD) of LETM1/MDM38 proteins.
Pssm-ID: 462258 [Multi-domain] Cd Length: 229 Bit Score: 37.46 E-value: 4.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 593416183 141 WDPEKQDKFLNKRKYYRPR----------------------KMNRFLKHVVDTNEISTKEEIQAVKEVFKN 189
Cdd:pfam07766 51 WSKKQKEEKLKKRLKARLEvakflqetveeslsdettelkeEFKEFFKKVRSGGEPPSNEEILKVAKLFKD 121
|
|
| |
