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Conserved domains on  [gi|446354016|ref|WP_000431871|]
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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: 567.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGAHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  355 YVYQNQPQGSNAFGRFIDKIYLNSVGWRGIRQRKTHLQMLIKQAVAHLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNLEELSALTPRPTLAIVSGLYELFPENEQVKNSLAGLANAIDPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354016  514 GILIYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVHDAGFDKCTQRIDVWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 5.42e-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: 246.36  E-value: 5.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVQDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  112 IAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPGLALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446354016  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLRSPLKELHLLPGFYHDTLGE 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: 567.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGAHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  355 YVYQNQPQGSNAFGRFIDKIYLNSVGWRGIRQRKTHLQMLIKQAVAHLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNLEELSALTPRPTLAIVSGLYELFPENEQVKNSLAGLANAIDPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354016  514 GILIYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVHDAGFDKCTQRIDVWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 5.42e-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: 246.36  E-value: 5.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVQDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  112 IAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPGLALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446354016  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLRSPLKELHLLPGFYHDTLGE 265
Cdd:pfam12146 159 ADPLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNE 236
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
9-281 6.13e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 153.23  E-value: 6.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   9 EHFFTTSDNTALFYRHWPTLlPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSV 88
Cdd:COG2267    5 LVTLPTRDGLRLRGRRWRPA-GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  89 QDVDEFVRFAASDSQvglEEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAfkvklyvplarpglalwhrlrglffin 168
Cdd:COG2267   84 DDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 169 syvkgrylthdrqrvasFNNDPLItrAIAVNILLDLyktseRIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLrSP 248
Cdd:COG2267  134 -----------------YRADPLL--GPSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SP 188

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446354016 249 LKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG2267  189 DVELVLLPGARHELLNEPAREEVLAAILAWLER 221
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 12-268 4.63e-16

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 80.32  E-value: 4.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  12 FTTSDNTALFYRHWPTLLPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVQDV 91
Cdd:PLN02652 115 FYGARRNALFCRSWAPAAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDT 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  92 DEFVRFAASDSQvGLEEVVVIAQSVGAVMVATWVHdyaPAIR----GLVLASPAFKVKLYVPLARPGLALWHRLRGLF-F 166
Cdd:PLN02652 195 EAFLEKIRSENP-GVPCFLFGHSTGGAVVLKAASY---PSIEdkleGIVLTSPALRVKPAHPIVGAVAPIFSLVAPRFqF 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 167 INSYVKGRYLTHDRQRVASFNNDPLI-TRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRL 245
Cdd:PLN02652 271 KGANKRGIPVSRDPAALLAKYSDPLVyTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEA 350

                        250       260
                 ....*....|....*....|...
gi 446354016 246 RSPLKELHLLPGFYHDTLGEENR 268
Cdd:PLN02652 351 ASRHKDIKLYDGFLHDLLFEPER 373
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 410-528 5.94e-05

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: 43.44  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALAnePAVSDILLRDYSELNVAQGQEMIAQRGMsgRVRFEQGDAFNLeelsaltPRPT----LAI 485
Cdd:COG2226   25 RVLDLGCGTGRLAL-ALA--ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL-------PFPDgsfdLVI 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446354016 486 VSGLYELFPENEQVknsLAGLANAIDPGGILIYT--GQPWHPQLE 528
Cdd:COG2226   93 SSFVLHHLPDPERA---LAEIARVLKPGGRLVVVdfSPPDLAELE 134
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-519 1.64e-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: 38.18  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALANEPAVSDILLrDYSELNVAQGQEMIAQRGMSgRVRFEQGDAFNLEELSAltPRPTLAIVSGL 489
Cdd:cd02440    1 RVLDLGCGTGALAL-ALASGPGARVTGV-DISPVALELARKAAAALLAD-NVEVLKGDAEELPPEAD--ESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 446354016 490 YELFPENeqVKNSLAGLANAIDPGGILIYT 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: 567.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  275 MQSFISRLYANKSQKFDYQHEDRTGPSADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGAHSAGLHLGMSTGFDSGSSLD 354
Cdd:pfam12147   1 IRRFILRSFAEPPQRFDLLDADRGGPSRDEADLLAAPLPWLSLRGLYWRATRAGLKLGGRLSKGLRLGLDTGFDSGSTLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  355 YVYQNQPQGSNAFGRFIDKIYLNSVGWRGIRQRKTHLQMLIKQAVAHLHAKGLAVRVVDIAAGHGRYVLDALANEPA-VS 433
Cdd:pfam12147  81 YVYRNQPRGRGPLGRLIDRQYLNAIGWRGIRQRKVHLEELLQQAIARLRAKGQPVRILDIAAGHGRYVLEALAKLPQrPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  434 DILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNLEELSALTPRPTLAIVSGLYELFPENEQVKNSLAGLANAIDPG 513
Cdd:pfam12147 161 SILLRDYSPLNVEQGNALIAAKGLEDIARFEQGDAFDPDSLAALTPQPTLAIVSGLYELFPDNDLVRRSLAGLAAAVEPG 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354016  514 GILIYTGQPWHPQLELIAGVLTSHKDGKPWVMRVRSQGEMDSLVHDAGFDKCTQRIDVWGIFTVSMAVR 582
Cdd:pfam12147 241 GYLIYTGQPWHPQLEMIARALTSHRDGEAWVMRRRSQAEMDELVEAAGFDKIDQRIDEWGIFTVSLARR 309
Hydrolase_4 pfam12146
Serine aminopeptidase, S33; This domain is found in bacteria and eukaryotes and is ...
 32-265 5.42e-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: 246.36  E-value: 5.42e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   32 AKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVQDVDEFVRFAASDSqvGLEEVVV 111
Cdd:pfam12146   3 PRAVVVLVHGLGEHSGRYAHLADALAAQGFAVYAYDHRGHGRSDGKRGHVPSFDDYVDDLDTFVDKIREEH--PGLPLFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  112 IAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYvpLARPGLALWHRLRGLFFINSYVKGR----YLTHDRQRVASFN 187
Cdd:pfam12146  81 LGHSMGGLIAALYALRYPDKVDGLILSAPALKIKPY--LAPPILKLLAKLLGKLFPRLRVPNNllpdSLSRDPEVVAAYA 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446354016  188 NDPLITRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLRSPLKELHLLPGFYHDTLGE 265
Cdd:pfam12146 159 ADPLVHGGISARTLYELLDAGERLLRRAAAITVPLLLLHGGADRVVDPAGSREFYERAGSTDKTLKLYPGLYHELLNE 236
PldB COG2267
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
9-281 6.13e-43

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


Pssm-ID: 441868 [Multi-domain]  Cd Length: 221  Bit Score: 153.23  E-value: 6.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   9 EHFFTTSDNTALFYRHWPTLlPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSV 88
Cdd:COG2267    5 LVTLPTRDGLRLRGRRWRPA-GSPRGTVVLVHGLGEHSGRYAELAEALAAAGYAVLAFDLRGHGRSDGPRGHVDSFDDYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  89 QDVDEFVRFAASDSQvglEEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAfkvklyvplarpglalwhrlrglffin 168
Cdd:COG2267   84 DDLRAALDALRARPG---LPVVLLGHSMGGLIALLYAARYPDRVAGLVLLAPA--------------------------- 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 169 syvkgrylthdrqrvasFNNDPLItrAIAVNILLDLyktseRIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLrSP 248
Cdd:COG2267  134 -----------------YRADPLL--GPSARWLRAL-----RLAEALARIDVPVLVLHGGADRVVPPEAARRLAARL-SP 188

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446354016 249 LKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG2267  189 DVELVLLPGARHELLNEPAREEVLAAILAWLER 221
YvaK COG1647
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
26-282 4.14e-16

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


Pssm-ID: 441253 [Multi-domain]  Cd Length: 246  Bit Score: 78.06  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  26 PTLLPGAKKVIVLFH--RGHEHSGRlqHIVDELAMPDTAFYAWDARGHGQTSGPrgyspSLARSVQDVDEFVRFAASDSQ 103
Cdd:COG1647    8 PFFLEGGRKGVLLLHgfTGSPAEMR--PLAEALAKAGYTVYAPRLPGHGTSPED-----LLKTTWEDWLEDVEEAYEILK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 104 VGLEEVVVIAQSVGAVMvATWVHDYAPAIRGLVLASPAFKVKlyvplaRPGLALWHRLRglfFINSYVKGRYLTHDRQRV 183
Cdd:COG1647   81 AGYDKVIVIGLSMGGLL-ALLLAARYPDVAGLVLLSPALKID------DPSAPLLPLLK---YLARSLRGIGSDIEDPEV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 184 ASFNNDPLITRAIAvnillDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLRSPLKELHLLPGFYHDTL 263
Cdd:COG1647  151 AEYAYDRTPLRALA-----ELQRLIREVRRDLPKITAPTLIIQSRKDEVVPPESARYIYERLGSPDKELVWLEDSGHVIT 225

                        250
                 ....*....|....*....
gi 446354016 264 GEENRAQAFEKMQSFISRL 282
Cdd:COG1647  226 LDKDREEVAEEILDFLERL 244
PLN02652 PLN02652
hydrolase; alpha/beta fold family protein
 12-268 4.63e-16

hydrolase; alpha/beta fold family protein


Pssm-ID: 215352 [Multi-domain]  Cd Length: 395  Bit Score: 80.32  E-value: 4.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  12 FTTSDNTALFYRHWPTLLPGAKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSVQDV 91
Cdd:PLN02652 115 FYGARRNALFCRSWAPAAGEMRGILIIIHGLNEHSGRYLHFAKQLTSCGFGVYAMDWIGHGGSDGLHGYVPSLDYVVEDT 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  92 DEFVRFAASDSQvGLEEVVVIAQSVGAVMVATWVHdyaPAIR----GLVLASPAFKVKLYVPLARPGLALWHRLRGLF-F 166
Cdd:PLN02652 195 EAFLEKIRSENP-GVPCFLFGHSTGGAVVLKAASY---PSIEdkleGIVLTSPALRVKPAHPIVGAVAPIFSLVAPRFqF 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 167 INSYVKGRYLTHDRQRVASFNNDPLI-TRAIAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRL 245
Cdd:PLN02652 271 KGANKRGIPVSRDPAALLAKYSDPLVyTGPIRVRTGHEILRISSYLTRNFKSVTVPFMVLHGTADRVTDPLASQDLYNEA 350

                        250       260
                 ....*....|....*....|...
gi 446354016 246 RSPLKELHLLPGFYHDTLGEENR 268
Cdd:PLN02652 351 ASRHKDIKLYDGFLHDLLFEPER 373
FrsA COG1073
Fermentation-respiration switch esterase FrsA, DUF1100 family [Signal transduction mechanisms]; ...
 11-281 6.49e-11

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


Pssm-ID: 440691 [Multi-domain]  Cd Length: 253  Bit Score: 63.01  E-value: 6.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  11 FFTTSDNTALFYRHW-PTLLPGAKKVIVLFH-RGHEHSGRLqHIVDELAMPDTAFYAWDARGHGQTSG-PRGYSpSLARs 87
Cdd:COG1073   14 TFKSRDGIKLAGDLYlPAGASKKYPAVVVAHgNGGVKEQRA-LYAQRLAELGFNVLAFDYRGYGESEGePREEG-SPER- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  88 vQDVDEFVRFAASDSQVGLEEVVVIAQSVGAVMVAtwvhDYA---PAIRGLVLASPafkvklyvplarpglalWHRLRGL 164
Cdd:COG1073   91 -RDARAAVDYLRTLPGVDPERIGLLGISLGGGYAL----NAAatdPRVKAVILDSP-----------------FTSLEDL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 165 FfinsyvkgrylthdRQRVASFNND-----PLITRAIAVNILLDLYktseRIVSDAAAITLPTQLLISGDDYVVHRQPQI 239
Cdd:COG1073  149 A--------------AQRAKEARGAylpgvPYLPNVRLASLLNDEF----DPLAKIEKISRPLLFIHGEKDEAVPFYMSE 210

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446354016 240 DFYQRLRSPlKELHLLPGFYHDTLGEENRAQAFEKMQSFISR 281
Cdd:COG1073  211 DLYEAAAEP-KELLIVPGAGHVDLYDRPEEEYFDKLAEFFKK 251
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 9-282 9.54e-11

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: 61.94  E-value: 9.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   9 EHFFTTSDNTALFYRHWPTllpgAKKVIVLFHrGHEHSGRL-QHIVDELAmPDTAFYAWDARGHGQTSGPRGySPSLARS 87
Cdd:COG0596    3 TPRFVTVDGVRLHYREAGP----DGPPVVLLH-GLPGSSYEwRPLIPALA-AGYRVIAPDLRGHGRSDKPAG-GYTLDDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  88 VQDVDEFVRfaasdsQVGLEEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAFKvKLYVPLARPGlalwhrlrglffi 167
Cdd:COG0596   76 ADDLAALLD------ALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVDEVLA-ALAEPLRRPG------------- 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 168 nsyvkgrylthdrqrvasfNNDPLITRAIAVNILLDLYktserivSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLrs 247
Cdd:COG0596  136 -------------------LAPEALAALLRALARTDLR-------ERLARITVPTLVIWGEKDPIVPPALARRLAELL-- 187

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 446354016 248 PLKELHLLPGFYHdTLGEENRAQAFEKMQSFISRL 282
Cdd:COG0596  188 PNAELVVLPGAGH-FPPLEQPEAFAAALRDFLARL 221
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
12-281 8.45e-08

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 53.48  E-value: 8.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  12 FTTSDNTALF-YRHWPtllPGAKK--VIVLFH-RGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPslars 87
Cdd:COG1506    2 FKSADGTTLPgWLYLP---ADGKKypVVVYVHgGPGSRDDSFLPLAQALASRGYAVLAPDYRGYGESAGDWGGDE----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  88 VQDVDEFVRFAASDSQVGLEEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPglalwhrlrglffi 167
Cdd:COG1506   74 VDDVLAAIDYLAARPYVDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLRSYYGTTRE-------------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 168 nsYVKGRYLTHDRQRVASFNNDPLitraiavnilldlyktserivSDAAAITLPTQLLISGDDYVVHRQPQIDFYQRLRS 247
Cdd:COG1506  140 --YTERLMGGPWEDPEAYAARSPL---------------------AYADKLKTPLLLIHGEADDRVPPEQAERLYEALKK 196

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 446354016 248 --PLKELHLLPGFYHDTLGEENRaQAFEKMQSFISR 281
Cdd:COG1506  197 agKPVELLVYPGEGHGFSGAGAP-DYLERILDFLDR 231
PHA02857 PHA02857
monoglyceride lipase; Provisional
 10-192 4.47e-07

monoglyceride lipase; Provisional


Pssm-ID: 165193 [Multi-domain]  Cd Length: 276  Bit Score: 51.81  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  10 HFFTTSDNTALFYRHW-PTLLPgaKKVIVLFHRGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSPSLARSV 88
Cdd:PHA02857   3 NCMFNLDNDYIYCKYWkPITYP--KALVFISHGAGEHSGRYEELAENISSLGILVFSHDHIGHGRSNGEKMMIDDFGVYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  89 QDVDEFVR-FAASDSQVgleEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKlyvPLARPGLaLWHRLRGLFFI 167
Cdd:PHA02857  81 RDVVQHVVtIKSTYPGV---PVFLLGHSMGATISILAAYKNPNLFTAMILMSPLVNAE---AVPRLNL-LAAKLMGIFYP 153

                        170       180
                 ....*....|....*....|....*...
gi 446354016 168 NSYVKG---RYLTHDRQRVASFNNDPLI 192
Cdd:PHA02857 154 NKIVGKlcpESVSRDMDEVYKYQYDPLV 181
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 34-266 2.89e-06

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: 49.04  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   34 KVIVLFHrGHEHSGRLQH-IVDELAMPDTAFYAWDARGHGQTSGPRGYSP-SLARSVQDVDEFVRfaasdsQVGLEEVVV 111
Cdd:pfam00561   1 PPVLLLH-GLPGSSDLWRkLAPALARDGFRVIALDLRGFGKSSRPKAQDDyRTDDLAEDLEYILE------ALGLEKVNL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  112 IAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPGLALWHRLRGLFFINSYVK------GRYLTHDRQRVAS 185
Cdd:pfam00561  74 VGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEADRFILALFPGFFDGFVADFAPNplgrlvAKLLALLLLRLRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  186 FNNDPLITRAIAVNIL-------------LDLYKTSERIvSDAAAITLPTQLLISGDDYVVHRQpQIDFYQRLrSPLKEL 252
Cdd:pfam00561 154 LKALPLLNKRFPSGDYalakslvtgallfIETWSTELRA-KFLGRLDEPTLIIWGDQDPLVPPQ-ALEKLAQL-FPNARL 230

                         250
                  ....*....|....
gi 446354016  253 HLLPGFYHDTLGEE 266
Cdd:pfam00561 231 VVIPDAGHFAFLEG 244
YpfH COG0400
Predicted esterase [General function prediction only];
30-156 4.69e-05

Predicted esterase [General function prediction only];


Pssm-ID: 440169 [Multi-domain]  Cd Length: 200  Bit Score: 44.51  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  30 PGAKKVIVLFH-RG-HEHSgrLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYS----------PSLARSVQDVDEFVRF 97
Cdd:COG0400    2 GPAAPLVVLLHgYGgDEED--LLPLAPELALPGAAVLAPRAPVPEGPGGRAWFDlsflegredeEGLAAAAEALAAFIDE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446354016  98 AASDSQVGLEEVVVIAQSVGAVMVATWVHDYAPAIRGLVLASPAFKVKLYVPLARPGLA 156
Cdd:COG0400   80 LEARYGIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSGYLPGEEALPAPEAALA 138
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 410-528 5.94e-05

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: 43.44  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALAnePAVSDILLRDYSELNVAQGQEMIAQRGMsgRVRFEQGDAFNLeelsaltPRPT----LAI 485
Cdd:COG2226   25 RVLDLGCGTGRLAL-ALA--ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDL-------PFPDgsfdLVI 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446354016 486 VSGLYELFPENEQVknsLAGLANAIDPGGILIYT--GQPWHPQLE 528
Cdd:COG2226   93 SSFVLHHLPDPERA---LAEIARVLKPGGRLVVVdfSPPDLAELE 134
PLN02298 PLN02298
hydrolase, alpha/beta fold family protein
 6-103 1.02e-04

hydrolase, alpha/beta fold family protein


Pssm-ID: 165939 [Multi-domain]  Cd Length: 330  Bit Score: 44.77  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   6 IPGEH-FFTTSDNTALFYRHWPTLLPGA-KKVIVLFH-RGHEHSGRLQHIVDELAMPDTAFYAWDARGHGQTSGPRGYSP 82
Cdd:PLN02298  30 IKGSKsFFTSPRGLSLFTRSWLPSSSSPpRALIFMVHgYGNDISWTFQSTAIFLAQMGFACFALDLEGHGRSEGLRAYVP 109

                         90       100
                 ....*....|....*....|.
gi 446354016  83 SLARSVQDVDEFVRFAASDSQ 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 1.99e-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: 41.54  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 395 IKQAVAHLHAKGLavRVVDIAAGHGRYvLDALANEPAvsDILLRDYSELNVAQGQEMIAQRgmsgRVRFEQGDafnLEEL 474
Cdd:COG2227   14 LAALLARLLPAGG--RVLDVGCGTGRL-ALALARRGA--DVTGVDISPEALEIARERAAEL----NVDFVQGD---LEDL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446354016 475 SALTPRPTLAIVSGLYELFPENEQVknsLAGLANAIDPGGILIYT 519
Cdd:COG2227   82 PLEDGSFDLVICSEVLEHLPDPAAL---LRELARLLKPGGLLLLS 123
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
410-517 2.16e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRyVLDALANEPAVSDILLRDYSElnvaqgqEMIAQ-RGMSGRVRFEQGDAFNLEelsaLTPRPTLAIVSG 488
Cdd:COG4106    4 RVLDLGCGTGR-LTALLAERFPGARVTGVDLSP-------EMLARaRARLPNVRFVVADLRDLD----PPEPFDLVVSNA 71

                         90       100
                 ....*....|....*....|....*....
gi 446354016 489 LYELFPENEQVknsLAGLANAIDPGGILI 517
Cdd:COG4106   72 ALHWLPDHAAL---LARLAAALAPGGVLA 97
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 410-517 2.83e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.45  E-value: 2.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALANEPAVS----DIllrdySELNVAQGQEMIAQRGMSGRVRFEQGDAFNLEElsaltPRPTLAI 485
Cdd:COG2230   54 RVLDIGCGWGGLAL-YLARRYGVRvtgvTL-----SPEQLEYARERAAEAGLADRVEVRLADYRDLPA-----DGQFDAI 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446354016 486 VS-GLYELFPeNEQVKNSLAGLANAIDPGGILI 517
Cdd:COG2230  123 VSiGMFEHVG-PENYPAYFAKVARLLKPGGRLL 154
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 36-257 5.63e-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: 41.69  E-value: 5.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016   36 IVLFHRGHEHSGRLQhivdELAMPDTAFYAWDARGHGQTSGPrgyspslARSVQDVDEFVRFAasDSQVGLEEVVVIAQS 115
Cdd:pfam12697   1 VVLVHGAGLSAAPLA----ALLAAGVAVLAPDLPGHGSSSPP-------PLDLADLADLAALL--DELGAARPVVLVGHS 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  116 VGAVMVATWVHdyAPAIRGLVLASPAFKVKLYVPLARPGLALWHRLRGLFFINSYVKGRYLTHDRQRVASFnndplitRA 195
Cdd:pfam12697  68 LGGAVALAAAA--AALVVGVLVAPLAAPPGLLAALLALLARLGAALAAPAWLAAESLARGFLDDLPADAEW-------AA 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446354016  196 IAVNILLDLYKTSERIVSDAAAITLPTQLLISGDDYVVHRQPQIdfyqRLRSPLKELHLLPG 257
Cdd:pfam12697 139 ALARLAALLAALALLPLAAWRDLPVPVLVLAEEDRLVPELAQRL----LAALAGARLVVLPG 196
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 408-476 8.29e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.09  E-value: 8.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446354016  408 AVRVVDIAAGHGRYVLDALANEPAVSDILLRDYSELNVAQGQEMIAQRGMSgRVRFEQGDAFNLEELSA 476
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDIEELPELLE 71
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 411-514 9.65e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 38.70  E-value: 9.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016  411 VVDIAAGHGRYVLdALANEpAVSDILLRDYSELNVAQGQEMIAQRGMsgRVRFEQGDAFNLEELSAltpRPTLAIVSGLY 490
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARR-GGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDG---SFDLVVSSGVL 73

                          90       100
                  ....*....|....*....|....
gi 446354016  491 ELFPENEQVKnSLAGLANAIDPGG 514
Cdd:pfam13649  74 HHLPDPDLEA-ALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 410-519 1.64e-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: 38.18  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALANEPAVSDILLrDYSELNVAQGQEMIAQRGMSgRVRFEQGDAFNLEELSAltPRPTLAIVSGL 489
Cdd:cd02440    1 RVLDLGCGTGALAL-ALASGPGARVTGV-DISPVALELARKAAAALLAD-NVEVLKGDAEELPPEAD--ESFDVIISDPP 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 446354016 490 YELFPENeqVKNSLAGLANAIDPGGILIYT 519
Cdd:cd02440   76 LHHLVED--LARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 410-520 1.70e-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: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 410 RVVDIAAGHGRYVLdALANEP--AVSDIllrDYSELNVAQGQEMIAQRGMsGRVRFEQGDAFNLEELSAltPRPTLAIVS 487
Cdd:COG0500   29 RVLDLGCGTGRNLL-ALAARFggRVIGI---DLSPEAIALARARAAKAGL-GNVEFLVADLAELDPLPA--ESFDLVVAF 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446354016 488 GLYELFPENEQVKnSLAGLANAIDPGGILIYTG 520
Cdd:COG0500  102 GVLHHLPPEEREA-LLRELARALKPGGVLLLSA 133
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
392-519 3.53e-03

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446354016 392 QMLIKQAVAHLHAKGLAvRVVDIAAGHGRyVLDALAnePAVSDILLRDYSElnvaqgqEMIAQ-RGMSGRVRFEQGDAFN 470
Cdd:COG4976   32 ALLAEELLARLPPGPFG-RVLDLGCGTGL-LGEALR--PRGYRLTGVDLSE-------EMLAKaREKGVYDRLLVADLAD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446354016 471 LEELSAltpRPTLAIVSGLYELFPENEQVknsLAGLANAIDPGGILIYT 519
Cdd:COG4976  101 LAEPDG---RFDLIVAADVLTYLGDLAAV---FAGVARALKPGGLFIFS 143
 
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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