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Conserved domains on  [gi|446353979|ref|WP_000431834|]
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bifunctional alpha/beta hydrolase/class I SAM-dependent methyltransferase [Escherichia coli]

Protein Classification

bifunctional alpha/beta hydrolase/class I SAM-dependent methyltransferase( domain architecture ID 12114409)

bifunctional alpha/beta hydrolase/class I SAM-dependent methyltransferase may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad and the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110|3.40.50.1820
EC:  2.1.1.-|3.-.-.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0016787
PubMed:  12504684|12826405|12369917|19508187
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_20 pfam12147
Putative methyltransferase; This domain is found in bacteria and eukaryotes and is ...
 275-582 0e+00

Putative methyltransferase; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The family shows homology to methyltransferases.


:

Pssm-ID: 432362  Cd Length: 309  Bit Score: 578.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGTHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  355 YVYQNQPQGSNAFGRLIDKIYLNSVGWRGIRQRKTHLQILIKQAVADLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNPEELSALTPRPTLAIVSGLYELFPGNEQVKNSLAGLANAIEPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446353979  514 GILLYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVRDAGFDKCTQRIDEWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 9.44e-78

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: 245.59  E-value: 9.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVRDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  112 IAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPALALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446353979  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLRSPLKELHLLPGFYHDTLGE 265
Cdd:pfam12146 159 ADPLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNE 236
 
Name Accession Description Interval E-value
Methyltransf_20 pfam12147
Putative methyltransferase; This domain is found in bacteria and eukaryotes and is ...
 275-582 0e+00

Putative methyltransferase; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The family shows homology to methyltransferases.


Pssm-ID: 432362  Cd Length: 309  Bit Score: 578.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGTHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  355 YVYQNQPQGSNAFGRLIDKIYLNSVGWRGIRQRKTHLQILIKQAVADLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNPEELSALTPRPTLAIVSGLYELFPGNEQVKNSLAGLANAIEPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446353979  514 GILLYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVRDAGFDKCTQRIDEWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 9.44e-78

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: 245.59  E-value: 9.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVRDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  112 IAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPALALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446353979  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLRSPLKELHLLPGFYHDTLGE 265
Cdd:pfam12146 159 ADPLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNE 236
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
9-281 1.78e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 154.77  E-value: 1.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   9 EHFFTTSDNTALFYRHWPAlQPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSV 88
Cdd:COG2267    5 LVTLPTRDGLRLRGRRWRP-AGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  89 RDVDEFVRFAASDSQvglEEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAfkvklyvplarpalalwhrlrglffin 168
Cdd:COG2267   84 DDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 169 syvkgrylthdrqrvasFNNDPLItrAIAVNILLDLyktseRIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLrSP 248
Cdd:COG2267  134 -----------------YRADPLL--GPSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SP 188

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446353979 249 LKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG2267  189 DVELVLLPGARHELLNEPAREEVLAAILAWLER 221
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 12-268 2.69e-16

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 81.09  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  12 FTTSDNTALFYRHWPALQPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVRDV 91
Cdd:PLN02652 115 FYGARRNALFCRSWAPAAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDT 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  92 DEFVRFAASDSQvGLEEVVVIAQSVGAVLVATWVHdyaPAIR----GLVLASPAFKVKLYVPLARPALALWHRLRGLF-F 166
Cdd:PLN02652 195 EAFLEKIRSENP-GVPCFLFGHSTGGAVVLKAASY---PSIEdkleGIVLTSPALRVKPAHPIVGAVAPIFSLVAPRFqF 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 167 INSYVKGRYLTHDRQRVASFNNDPLI-TRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRL 245
Cdd:PLN02652 271 KGANKRGIPVSRDPAALLAKYSDPLVyTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEA 350

                        250       260
                 ....*....|....*....|...
gi 446353979 246 RSPLKELHLLPGFYHDTLGEENR 268
Cdd:PLN02652 351 ASRHKDIKLYDGFLHDLLFEPER 373
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 397-517 1.80e-04

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.22  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 397 QAVADLHAKGLAV----RVVDIAAGHGRYVLdALANEPAVS----DIllrdySELNVAQGQEMIAQRGMSGRVRFEQGDA 468
Cdd:COG2230   37 EAKLDLILRKLGLkpgmRVLDIGCGWGGLAL-YLARRYGVRvtgvTL-----SPEQLEYARERAAEAGLADRVEVRLADY 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446353979 469 FNpeelsaLTPRPTL-AIVS-GLYELFpGNEQVKNSLAGLANAIEPGGILL 517
Cdd:COG2230  111 RD------LPADGQFdAIVSiGMFEHV-GPENYPAYFAKVARLLKPGGRLL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-519 4.44e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.02  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 410 RVVDIAAGHGRYVLdALANEPAVSDILLrDYSELNVAQGQEMIAQRGMSgRVRFEQGDAFNPEELSAltPRPTLAIVSGL 489
Cdd:cd02440    1 RVLDLGCGTGALAL-ALASGPGARVTGV-DISPVALELARKAAAALLAD-NVEVLKGDAEELPPEAD--ESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 446353979 490 YELFPGNeqVKNSLAGLANAIEPGGILLYT 519
Cdd:cd02440   76 LHHLVED--LARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
Methyltransf_20 pfam12147
Putative methyltransferase; This domain is found in bacteria and eukaryotes and is ...
 275-582 0e+00

Putative methyltransferase; This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The family shows homology to methyltransferases.


Pssm-ID: 432362  Cd Length: 309  Bit Score: 578.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGTHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  355 YVYQNQPQGSNAFGRLIDKIYLNSVGWRGIRQRKTHLQILIKQAVADLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNPEELSALTPRPTLAIVSGLYELFPGNEQVKNSLAGLANAIEPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446353979  514 GILLYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVRDAGFDKCTQRIDEWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 9.44e-78

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: 245.59  E-value: 9.44e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVRDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  112 IAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPALALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446353979  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLRSPLKELHLLPGFYHDTLGE 265
Cdd:pfam12146 159 ADPLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNE 236
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
9-281 1.78e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 154.77  E-value: 1.78e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   9 EHFFTTSDNTALFYRHWPAlQPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSV 88
Cdd:COG2267    5 LVTLPTRDGLRLRGRRWRP-AGSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  89 RDVDEFVRFAASDSQvglEEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAfkvklyvplarpalalwhrlrglffin 168
Cdd:COG2267   84 DDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 169 syvkgrylthdrqrvasFNNDPLItrAIAVNILLDLyktseRIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLrSP 248
Cdd:COG2267  134 -----------------YRADPLL--GPSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SP 188

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446353979 249 LKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG2267  189 DVELVLLPGARHELLNEPAREEVLAAILAWLER 221
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 12-268 2.69e-16

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 81.09  E-value: 2.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  12 FTTSDNTALFYRHWPALQPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVRDV 91
Cdd:PLN02652 115 FYGARRNALFCRSWAPAAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDT 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  92 DEFVRFAASDSQvGLEEVVVIAQSVGAVLVATWVHdyaPAIR----GLVLASPAFKVKLYVPLARPALALWHRLRGLF-F 166
Cdd:PLN02652 195 EAFLEKIRSENP-GVPCFLFGHSTGGAVVLKAASY---PSIEdkleGIVLTSPALRVKPAHPIVGAVAPIFSLVAPRFqF 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 167 INSYVKGRYLTHDRQRVASFNNDPLI-TRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRL 245
Cdd:PLN02652 271 KGANKRGIPVSRDPAALLAKYSDPLVyTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEA 350

                        250       260
                 ....*....|....*....|...
gi 446353979 246 RSPLKELHLLPGFYHDTLGEENR 268
Cdd:PLN02652 351 ASRHKDIKLYDGFLHDLLFEPER 373
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
26-282 3.73e-16

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 78.44  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  26 PALQPGAKKVIVLFH--RGHEHSGRlqHIVDELAMPDTAFYAWDARGHGQTSGPrgyspSLARSVRDVDEFVRFAASDSQ 103
Cdd:COG1647    8 PFFLEGGRKGVLLLHgfTGSPAEMR--PLAEALAKAGYTVYAPRLPGHGTSPED-----LLKTTWEDWLEDVEEAYEILK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 104 VGLEEVVVIAQSVGAVLvATWVHDYAPAIRGLVLASPAFKVKlyvplaRPALALWHRLRglfFINSYVKGRYLTHDRQRV 183
Cdd:COG1647   81 AGYDKVIVIGLSMGGLL-ALLLAARYPDVAGLVLLSPALKID------DPSAPLLPLLK---YLARSLRGIGSDIEDPEV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 184 ASFNNDPLITRAIAvnillDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLRSPLKELHLLPGFYHDTL 263
Cdd:COG1647  151 AEYAYDRTPLRALA-----ELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVIT 225

                        250
                 ....*....|....*....
gi 446353979 264 GEENRAQAFEKMQSFISRL 282
Cdd:COG1647  226 LDKDREEVAEEILDFLERL 244
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 11-281 3.72e-11

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 63.78  E-value: 3.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  11 FFTTSDNTALFYRHW-PALQPGAKKVIVLFH-RGHEHSGRLqHIVDELAMPDTAFYAWDARGHGQTSG-PRGYSpSLARs 87
Cdd:COG1073   14 TFKSRDGIKLAGDLYlPAGASKKYPAVVVAHgNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGePREEG-SPER- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  88 vRDVDEFVRFAASDSQVGLEEVVVIAQSVGAVLVAtwvhDYA---PAIRGLVLASPafkvklYVPLARPALALWHRLRGl 164
Cdd:COG1073   91 -RDARAAVDYLRTLPGVDPERIGLLGISLGGGYAL----NAAatdPRVKAVILDSP------FTSLEDLAAQRAKEARG- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 165 ffinsyvkgrylthdrqrvASFNNDPLITRAIAVNILLDLYktseRIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYHR 244
Cdd:COG1073  159 -------------------AYLPGVPYLPNVRLASLLNDEF----DPLAKIEKISRPLLFIHGEKDEAVPFYMSEDLYEA 215

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446353979 245 LRSPlKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG1073  216 AAEP-KELLIVPGAGHVDLYDRPEEEYFDKLAEFFKK 251
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 9-282 2.49e-10

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: 60.79  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   9 EHFFTTSDNTALFYRHWPAlqpgAKKVIVLFHrGHEHSGRL-QHIVDELAmPDTAFYAWDARGHGQTSGPRGySPSLARS 87
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGP----DGPPVVLLH-GLPGSSYEwRPLIPALA-AGYRVIAPDLRGHGRSDKPAG-GYTLDDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  88 VRDVDEFVRfaasdsQVGLEEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAFKvKLYVPLARPAlalwhrlrglffi 167
Cdd:COG0596   76 ADDLAALLD------ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-ALAEPLRRPG------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 168 nsyvkgrylthdrqrvasfNNDPLITRAIAVNILLDLYktserivSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLrs 247
Cdd:COG0596  136 -------------------LAPEALAALLRALARTDLR-------ERLARITVPTLVIWGEKDPIVPPALARRLAELL-- 187

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446353979 248 PLKELHLLPGFYHdTLGEENRAQAFEKMQSFISRL 282
Cdd:COG0596  188 PNAELVVLPGAGH-FPPLEQPEAFAAALRDFLARL 221
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-281 8.14e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 8.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  12 FTTSDNTALFYRHWPALQPGAKKVIVLFH-RGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPslarsVRD 90
Cdd:COG1506    2 FKSADGTTLPGWLYLPADGKKYPVVVYVHgGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE-----VDD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  91 VDEFVRFAASDSQVGLEEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPalalwhrlrglffinsY 170
Cdd:COG1506   77 VLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTRE----------------Y 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 171 VKGRYLTHDRQRVASFNNDPLitraiavnilldlyktserivSDAAAITLPTQLLISGDDYVVHRQPQIDFYHRLRS--P 248
Cdd:COG1506  141 TERLMGGPWEDPEAYAARSPL---------------------AYADKLKTPLLLIHGEADDRVPPEQAERLYEALKKagK 199

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446353979 249 LKELHLLPGFYHDTLGEENRaQAFEKMQSFISR 281
Cdd:COG1506  200 PVELLVYPGEGHGFSGAGAP-DYLERILDFLDR 231
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 34-266 7.33e-07

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: 50.58  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   34 KVIVLFHrGHEHSGRLQH-IVDELAMPDTAFYAWDARGHGQTSGPRGYSP-SLARSVRDVDEFVRfaasdsQVGLEEVVV 111
Cdd:pfam00561   1 PPVLLLH-GLPGSSDLWRkLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILE------ALGLEKVNL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  112 IAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPALALWHRLRGLFFINSYVK------GRYLTHDRQRVAS 185
Cdd:pfam00561  74 VGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNplgrlvAKLLALLLLRLRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  186 FNNDPLITRAIAVNIL-------------LDLYKTSERIvSDAAAITLPTQLLISGDDYVVHRQpQIDFYHRLrSPLKEL 252
Cdd:pfam00561 154 LKALPLLNKRFPSGDYalakslvtgallfIETWSTELRA-KFLGRLDEPTLIIWGDQDPLVPPQ-ALEKLAQL-FPNARL 230

                         250
                  ....*....|....
gi 446353979  253 HLLPGFYHDTLGEE 266
Cdd:pfam00561 231 VVIPDAGHFAFLEG 244
PHA02857 PHA02857
monoglyceride lipase; Provisional
 10-192 8.50e-07

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 50.65  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  10 HFFTTSDNTALFYRHWpALQPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVR 89
Cdd:PHA02857   3 NCMFNLDNDYIYCKYW-KPITYPKALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYVR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  90 DVDEFVR-FAASDSQVgleEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKlyvPLARPALaLWHRLRGLFFIN 168
Cdd:PHA02857  82 DVVQHVVtIKSTYPGV---PVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAE---AVPRLNL-LAAKLMGIFYPN 154

                        170       180
                 ....*....|....*....|....*..
gi 446353979 169 SYVKG---RYLTHDRQRVASFNNDPLI 192
Cdd:PHA02857 155 KIVGKlcpESVSRDMDEVYKYQYDPLV 181
PLN02385 PLN02385
hydrolase; alpha/beta fold family protein
 9-289 5.93e-05

hydrolase; alpha/beta fold family protein


Pssm-ID: 215216 [Multi-domain]  Cd Length: 349  Bit Score: 45.51  E-value: 5.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   9 EHFFTTSDNTALFYRHW-PalQPGAKKVIVLFHRGHEHSGR--LQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLA 85
Cdd:PLN02385  63 ESYEVNSRGVEIFSKSWlP--ENSRPKAAVCFCHGYGDTCTffFEGIARKIASSGYGVFAMDYPGFGLSEGLHGYIPSFD 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  86 RSVRDVDE-FVRFAASDSQVGLEEvVVIAQSVGAVlVATWVHDYAP-AIRGLVLASPAFKVKLYV---PLARPALALWHR 160
Cdd:PLN02385 141 DLVDDVIEhYSKIKGNPEFRGLPS-FLFGQSMGGA-VALKVHLKQPnAWDGAILVAPMCKIADDVvppPLVLQILILLAN 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 161 L---RGLFFINSYVKGRYLTHDRQRVASFNndplitrAIAVN------ILLDLYKTSERIVSDAAAITLPTQLLISGDDY 231
Cdd:PLN02385 219 LlpkAKLVPQKDLAELAFRDLKKRKMAEYN-------VIAYKdkprlrTAVELLRTTQEIEMQLEEVSLPLLILHGEADK 291

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446353979 232 VVHRQPQIDFYHRLRSPLKELHLLPGFYHDTLGEENRAQAFEKMQSFISRLYANKSQK 289
Cdd:PLN02385 292 VTDPSVSKFLYEKASSSDKKLKLYEDAYHSILEGEPDEMIFQVLDDIISWLDSHSTQK 349
YpfH COG0400
Predicted esterase [General function prediction only];
30-156 7.59e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 44.13  E-value: 7.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  30 PGAKKVIVLFH-RG-HEHSgrLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYS----------PSLARSVRDVDEFVRF 97
Cdd:COG0400    2 GPAAPLVVLLHgYGgDEED--LLPLAPELALPGAAVLAPRAPVPEGPGGRAWFDlsflegredeEGLAAAAEALAAFIDE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446353979  98 AASDSQVGLEEVVVIAQSVGAVLVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPALA 156
Cdd:COG0400   80 LEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 36-257 1.46e-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: 43.23  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   36 IVLFHRGHEHSGRLQhivdELAMPDTAFYAWDARGHGQTSGPrgyspslARSVRDVDEFVRFAasDSQVGLEEVVVIAQS 115
Cdd:pfam12697   1 VVLVHGAGLSAAPLA----ALLAAGVAVLAPDLPGHGSSSPP-------PLDLADLADLAALL--DELGAARPVVLVGHS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  116 VGAVLVATWVHdyAPAIRGLVLASPAFKVKLYVPLARPALALWHRLRGLFFINSYVKGRYLTHDRQRVASFnndplitRA 195
Cdd:pfam12697  68 LGGAVALAAAA--AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEW-------AA 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446353979  196 IAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIdfyhRLRSPLKELHLLPG 257
Cdd:pfam12697 139 ALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRL----LAALAGARLVVLPG 196
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 397-517 1.80e-04

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.22  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 397 QAVADLHAKGLAV----RVVDIAAGHGRYVLdALANEPAVS----DIllrdySELNVAQGQEMIAQRGMSGRVRFEQGDA 468
Cdd:COG2230   37 EAKLDLILRKLGLkpgmRVLDIGCGWGGLAL-YLARRYGVRvtgvTL-----SPEQLEYARERAAEAGLADRVEVRLADY 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446353979 469 FNpeelsaLTPRPTL-AIVS-GLYELFpGNEQVKNSLAGLANAIEPGGILL 517
Cdd:COG2230  111 RD------LPADGQFdAIVSiGMFEHV-GPENYPAYFAKVARLLKPGGRLL 154
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 6-103 2.02e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 43.61  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979   6 IPGEH-FFTTSDNTALFYRHWPALQPGA-KKVIVLFH-RGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSP 82
Cdd:PLN02298  30 IKGSKsFFTSPRGLSLFTRSWLPSSSSPpRALIFMVHgYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVP 109

                         90       100
                 ....*....|....*....|.
gi 446353979  83 SLARSVRDVDEFVRFAASDSQ 103
Cdd:PLN02298 110 NVDLVVEDCLSFFNSVKQREE 130
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 395-519 6.44e-04

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 40.00  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 395 IKQAVADLHAKGLavRVVDIAAGHGRYvLDALANEPAvsDILLRDYSELNVAQGQEMIAQRgmsgRVRFEQGDAfnpEEL 474
Cdd:COG2227   14 LAALLARLLPAGG--RVLDVGCGTGRL-ALALARRGA--DVTGVDISPEALEIARERAAEL----NVDFVQGDL---EDL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446353979 475 SALTPRPTLAIVSGLYELFPGNEQVknsLAGLANAIEPGGILLYT 519
Cdd:COG2227   82 PLEDGSFDLVICSEVLEHLPDPAAL---LRELARLLKPGGLLLLS 123
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 410-528 6.78e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 40.36  E-value: 6.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 410 RVVDIAAGHGRYVLdALAnePAVSDILLRDYSELNVAQGQEMIAQRGMsgRVRFEQGDAfnpEELSALTPRPTLAIVSGL 489
Cdd:COG2226   25 RVLDLGCGTGRLAL-ALA--ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDA---EDLPFPDGSFDLVISSFV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446353979 490 YELFPGNEQVknsLAGLANAIEPGGILLYT--GQPWHPQLE 528
Cdd:COG2226   97 LHHLPDPERA---LAEIARVLKPGGRLVVVdfSPPDLAELE 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 411-514 7.35e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979  411 VVDIAAGHGRYVLdALANEpAVSDILLRDYSELNVAQGQEMIAQRGMsgRVRFEQGDAfnpEELSALTPRPTLAIVSGLY 490
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARR-GGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDA---EDLPFPDGSFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|....
gi 446353979  491 ELFPgNEQVKNSLAGLANAIEPGG 514
Cdd:pfam13649  74 HHLP-DPDLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
410-517 1.77e-03

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.88  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 410 RVVDIAAGHGRyVLDALANEPAVSDILLRDYSElnvaqgqEMIAQ-RGMSGRVRFEQGDAFNpeelsaLTPRPTL-AIVS 487
Cdd:COG4106    4 RVLDLGCGTGR-LTALLAERFPGARVTGVDLSP-------EMLARaRARLPNVRFVVADLRD------LDPPEPFdLVVS 69

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446353979 488 G--LYELfPGNEQVknsLAGLANAIEPGGILL 517
Cdd:COG4106   70 NaaLHWL-PDHAAL---LARLAAALAPGGVLA 97
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 410-520 1.99e-03

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 39.90  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 410 RVVDIAAGHGRYVLD-ALANEPAVSDIllrDYSELNVAQGQEMIAQRGMsGRVRFEQGDAFNPEELSAltPRPTLAIVSG 488
Cdd:COG0500   29 RVLDLGCGTGRNLLAlAARFGGRVIGI---DLSPEAIALARARAAKAGL-GNVEFLVADLAELDPLPA--ESFDLVVAFG 102

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446353979 489 LYELFPGNEQVKnSLAGLANAIEPGGILLYTG 520
Cdd:COG0500  103 VLHHLPPEEREA-LLRELARALKPGGVLLLSA 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-519 4.44e-03

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 37.02  E-value: 4.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446353979 410 RVVDIAAGHGRYVLdALANEPAVSDILLrDYSELNVAQGQEMIAQRGMSgRVRFEQGDAFNPEELSAltPRPTLAIVSGL 489
Cdd:cd02440    1 RVLDLGCGTGALAL-ALASGPGARVTGV-DISPVALELARKAAAALLAD-NVEVLKGDAEELPPEAD--ESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 446353979 490 YELFPGNeqVKNSLAGLANAIEPGGILLYT 519
Cdd:cd02440   76 LHHLVED--LARFLEEARRLLKPGGVLVLT 103
 
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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