NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|640471004|ref|WP_024911586|]
View 

malonyl-ACP O-methyltransferase BioC [Chania multitudinisentens]

Protein Classification

malonyl-ACP O-methyltransferase BioC( domain architecture ID 1007885)

malonyl-ACP O-methyltransferase BioC converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM)

EC:  2.1.1.197
Gene Ontology:  GO:0010340|GO:0009102|GO:1904047|GO:0032259|GO:0102130|GO:0008757

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK10258 super family cl30595
biotin biosynthesis protein BioC; Provisional
 8-255 4.49e-90

biotin biosynthesis protein BioC; Provisional


The actual alignment was detected with superfamily member PRK10258:

Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 266.62  E-value: 4.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   8 VNKQAVAAAFSRAAEGYDAAAVLQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQ 87
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  88 QAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQVDGERHVN 167
Cdd:PRK10258  84 DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERPHAN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004 168 DFLPSAQIAAACGDYRHHLQEAWQTLEYPDVMTLLRSLKGIGATHLHQGRNMGLLSRQRLAALQAAYPRHHGLFPLSYRL 247
Cdd:PRK10258 164 RFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHL 243


                 ....*...
gi 640471004 248 VYGVIYRD 255
Cdd:PRK10258 244 FLGVIERD 251
 
Name Accession Description Interval E-value
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 8-255 4.49e-90

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 266.62  E-value: 4.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   8 VNKQAVAAAFSRAAEGYDAAAVLQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQ 87
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  88 QAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQVDGERHVN 167
Cdd:PRK10258  84 DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERPHAN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004 168 DFLPSAQIAAACGDYRHHLQEAWQTLEYPDVMTLLRSLKGIGATHLHQGRNMGLLSRQRLAALQAAYPRHHGLFPLSYRL 247
Cdd:PRK10258 164 RFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHL 243


                 ....*...
gi 640471004 248 VYGVIYRD 255
Cdd:PRK10258 244 FLGVIERD 251
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 24-254 6.31e-68

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 209.84  E-value: 6.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   24 YDAAAVLQREVGERLLKMGRNHPGQQ---LLDAGCGTGYFSRRWRELGKQV--TALDLAPGMLAFARQQQAADR-YLLGD 97
Cdd:TIGR02072   9 YDRHAKIQREMAKRLLALLKEKGIFIpasVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTKLSENVqFICGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   98 IENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQvdgerHVNDFLPSAQIAA 177
Cdd:TIGR02072  89 AEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGLRYLSLDELKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  178 ACGDYRHHLQ--EAWQTLEYPDVMTLLRSLKGIGATHLHQGRnmglLSRQRLAALQAAYPRH---HGlFPLSYRLVYGVI 252
Cdd:TIGR02072 164 LLKNSFELLTleEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQEfqpDG-LPLTYHVVYGIA 238


                  ..
gi 640471004  253 YR 254
Cdd:TIGR02072 239 KK 240
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 24-160 1.76e-35

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: 123.57  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  24 YDAAAVlQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAAD----RYLLGDIE 99
Cdd:COG2226    1 FDRVAA-RYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnvEFVVGDAE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640471004 100 NIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQV 160
Cdd:COG2226   80 DLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-142 1.09e-30

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 109.68  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   51 LDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQ--QQAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALA 128
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 640471004  129 ELYRVTRPGGMILF 142
Cdd:pfam08241  81 EIARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-143 1.13e-14

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: 67.84  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  50 LLDAGCGTGYFSRRWREL-GKQVTALDLAPGMLAFARQQQAAD-----RYLLGDIENIPLPA-AAVDICFSSLVVQW-CS 121
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPEAdESFDVIISDPPLHHlVE 81

                         90       100
                 ....*....|....*....|..
gi 640471004 122 DLRRALAELYRVTRPGGMILFS 143
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 8-255 4.49e-90

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 266.62  E-value: 4.49e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   8 VNKQAVAAAFSRAAEGYDAAAVLQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQ 87
Cdd:PRK10258   4 VNKQAIAAAFGRAAAHYEQHAELQRQSADALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  88 QAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQVDGERHVN 167
Cdd:PRK10258  84 DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQAWQAVDERPHAN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004 168 DFLPSAQIAAACGDYRHHLQEAWQTLEYPDVMTLLRSLKGIGATHLHQGRNMGLLSRQRLAALQAAYPRHHGLFPLSYRL 247
Cdd:PRK10258 164 RFLPPDAIEQALNGWRYQHHIQPITLWFDDALSAMRSLKGIGATHLHEGRDPRILTRSQLQRLQLAWPQQQGRYPLTYHL 243


                 ....*...
gi 640471004 248 VYGVIYRD 255
Cdd:PRK10258 244 FLGVIERD 251
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 24-254 6.31e-68

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 209.84  E-value: 6.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   24 YDAAAVLQREVGERLLKMGRNHPGQQ---LLDAGCGTGYFSRRWRELGKQV--TALDLAPGMLAFARQQQAADR-YLLGD 97
Cdd:TIGR02072   9 YDRHAKIQREMAKRLLALLKEKGIFIpasVLDIGCGTGYLTRALLKRFPQAefIALDISAGMLAQAKTKLSENVqFICGD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   98 IENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQvdgerHVNDFLPSAQIAA 177
Cdd:TIGR02072  89 AEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQ-----HGLRYLSLDELKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  178 ACGDYRHHLQ--EAWQTLEYPDVMTLLRSLKGIGATHLHQGRnmglLSRQRLAALQAAYPRH---HGlFPLSYRLVYGVI 252
Cdd:TIGR02072 164 LLKNSFELLTleEELITLSFDDPLDVLRHLKKTGANGLSSGR----TSRKQLKAFLERYEQEfqpDG-LPLTYHVVYGIA 238


                  ..
gi 640471004  253 YR 254
Cdd:TIGR02072 239 KK 240
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 24-160 1.76e-35

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: 123.57  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  24 YDAAAVlQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAAD----RYLLGDIE 99
Cdd:COG2226    1 FDRVAA-RYDGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnvEFVVGDAE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 640471004 100 NIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLYQLADAWQQV 160
Cdd:COG2226   80 DLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELLAEA 140
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-142 1.09e-30

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 109.68  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   51 LDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQ--QQAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALA 128
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREkaPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPERALR 80

                          90
                  ....*....|....
gi 640471004  129 ELYRVTRPGGMILF 142
Cdd:pfam08241  81 EIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-144 3.01e-27

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: 101.63  E-value: 3.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAADR--YLLGDIENIPLPAAAVDICFSSLVVQWCSDL 123
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNvdFVQGDLEDLPLEDGSFDLVICSEVLEHLPDP 103

                         90       100
                 ....*....|....*....|.
gi 640471004 124 RRALAELYRVTRPGGMILFST 144
Cdd:COG2227  104 AALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 51-138 2.28e-26

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 98.40  E-value: 2.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   51 LDAGCGTGYFSRRW-RELGKQVTALDLAPGMLAFARQQQAAD----RYLLGDIENIPLPAAAVDICFSSLVVQWCS--DL 123
Cdd:pfam13649   2 LDLGCGTGRLTLALaRRGGARVTGVDLSPEMLERARERAAEAglnvEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPdpDL 81

                          90
                  ....*....|....*
gi 640471004  124 RRALAELYRVTRPGG 138
Cdd:pfam13649  82 EAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
24-148 1.88e-22

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 90.83  E-value: 1.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  24 YDAAAV------LQREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAADRYLLGD 97
Cdd:COG4976   18 YDAALVedlgyeAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVYDRLLVAD 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 640471004  98 IENIPLPAAAVDICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATD 148
Cdd:COG4976   98 LADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDAD 148
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-144 3.33e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 87.57  E-value: 3.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTGYFSRRWREL--GKQVTALDLAPGMLAFARQQQAADRYLLGDIENIPLPAAAvDICFSSLVVQWCSDL 123
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLPNVRFVVADLRDLDPPEPF-DLVVSNAALHWLPDH 79

                         90       100
                 ....*....|....*....|.
gi 640471004 124 RRALAELYRVTRPGGMILFST 144
Cdd:COG4106   80 AALLARLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
 46-141 3.36e-20

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 86.14  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTGYFSRrwrELGKQVT------ALDLAPGMLAFARQQQAAD----RYLLGDIENIPLPAAAVDICFSSL 115
Cdd:PRK08317  19 PGDRVLDVGCGPGNDAR---ELARRVGpegrvvGIDRSEAMLALAKERAAGLgpnvEFVRGDADGLPFPDGSFDAVRSDR 95

                         90       100
                 ....*....|....*....|....*.
gi 640471004 116 VVQWCSDLRRALAELYRVTRPGGMIL 141
Cdd:PRK08317  96 VLQHLEDPARALAEIARVLRPGGRVV 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 46-157 7.50e-17

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 77.12  E-value: 7.50e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTGYFSRRW-RELGK--QVTALDLAPGMLAFARQQQAADR------YLLGDIENIPLPAAAVD---ICFS 113
Cdd:PRK00216  51 PGDKVLDLACGTGDLAIALaKAVGKtgEVVGLDFSEGMLAVGREKLRDLGlsgnveFVQGDAEALPFPDNSFDavtIAFG 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 640471004 114 sL--VVqwcsDLRRALAELYRVTRPGG--MIL-FSTLATDSLYQLADAW 157
Cdd:PRK00216 131 -LrnVP----DIDKALREMYRVLKPGGrlVILeFSKPTNPPLKKAYDFY 174
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 36-157 1.05e-15

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 73.84  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   36 ERLLKMGRNHPGQQLLDAGCGTGYFSRRWRELG---KQVTALDLAPGMLAFARQQQAAD---RYLLGDIENIPLPAAAVD 109
Cdd:TIGR01934  29 RRAVKLIGVFKGQKVLDVACGTGDLAIELAKSApdrGKVTGVDFSSEMLEVAKKKSELPlniEFIQADAEALPFEDNSFD 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 640471004  110 ICFSSLVVQWCSDLRRALAELYRVTRPGGMIL---FSTLATDSLYQLADAW 157
Cdd:TIGR01934 109 AVTIAFGLRNVTDIQKALREMYRVLKPGGRLVileFSKPANALLKKFYKFY 159
arsM PRK11873
arsenite methyltransferase;
45-143 1.20e-15

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 74.21  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  45 HPGQQLLDAGCGTGY--F--SRRWRELGKqVTALDLAPGMLAFARQQQAADRY-----LLGDIENIPLPAAAVDICFSSL 115
Cdd:PRK11873  76 KPGETVLDLGSGGGFdcFlaARRVGPTGK-VIGVDMTPEMLAKARANARKAGYtnvefRLGEIEALPVADNSVDVIISNC 154

                         90       100
                 ....*....|....*....|....*...
gi 640471004 116 VVQWCSDLRRALAELYRVTRPGGMILFS 143
Cdd:PRK11873 155 VINLSPDKERVFKEAFRVLKPGGRFAIS 182
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 50-143 1.13e-14

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: 67.84  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  50 LLDAGCGTGYFSRRWREL-GKQVTALDLAPGMLAFARQQQAAD-----RYLLGDIENIPLPA-AAVDICFSSLVVQW-CS 121
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALladnvEVLKGDAEELPPEAdESFDVIISDPPLHHlVE 81

                         90       100
                 ....*....|....*....|..
gi 640471004 122 DLRRALAELYRVTRPGGMILFS 143
Cdd:cd02440   82 DLARFLEEARRLLKPGGVLVLT 103
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-170 6.75e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 68.40  E-value: 6.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTGYFSRRWREL-GKQVTALDLAPGMLAFARQQQAAD-----RYLLGDIENI-PLPAAAVDICFSSLVVQ 118
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAglgnvEFLVADLAELdPLPAESFDLVVAFGVLH 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 640471004 119 WCS--DLRRALAELYRVTRPGG---MILFSTLATDSLYQLADAWQQVDGERHVNDFL 170
Cdd:COG0500  106 HLPpeEREALLRELARALKPGGvllLSASDAAAALSLARLLLLATASLLELLLLLRL 162
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 36-144 8.23e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.88  E-value: 8.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  36 ERLLKMGRNHPGQQLLDAGCGTGYFSRRW-RELGKQVTALDLAPGMLAFARQQQAAD------RYLLGDIENIPLPaAAV 108
Cdd:COG2230   41 DLILRKLGLKPGMRVLDIGCGWGGLALYLaRRYGVRVTGVTLSPEQLEYARERAAEAgladrvEVRLADYRDLPAD-GQF 119

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 640471004 109 DICFSSLVVQWCSD--LRRALAELYRVTRPGGMILFST 144
Cdd:COG2230  120 DAIVSIGMFEHVGPenYPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 51-140 4.00e-13

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 63.54  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   51 LDAGCGTGYFSRRWREL--GKQVTALDLAPGMLAFARQQQAADRYLLGDIENIP------LPAAAVDICFSSLVVQWCSD 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAARERLAALGLLNAVRVELFqldlgeLDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 640471004  123 LRRALAELYRVTRPGGMI 140
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 45-159 5.24e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 62.05  E-value: 5.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   45 HPGQQLLDAGCGTGYFSRRWREL---GKQVTALDLAPGMLAFAR---QQQAADRY--LLGDIENIP--LPAAAVDICFSS 114
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARenaQKLGFDNVefEQGDIEELPelLEDDKFDVVISN 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 640471004  115 LVVQWCSDLRRALAELYRVTRPGGMILFSTLatDSLYQLADAWQQ 159
Cdd:pfam13847  82 CVLNHIPDPDKVLQEILRVLKPGGRLIISDP--DSLAELPAHVKE 124
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
46-140 4.71e-10

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 58.44  E-value: 4.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQL--LDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFArQQQAADRYLLGDIENIPLPA--------AAVDICFSSL 115
Cdd:PRK11036  42 PPRPLrvLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRA-KQAAEAKGVSDNMQFIHCAAqdiaqhleTPVDLILFHA 120

                         90       100
                 ....*....|....*....|....*
gi 640471004 116 VVQWCSDLRRALAELYRVTRPGGMI 140
Cdd:PRK11036 121 VLEWVADPKSVLQTLWSVLRPGGAL 145
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 39-143 1.38e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 56.77  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  39 LKMGRNHPGQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAAD------RYLLGDIENIPLPAAAVdICF 112
Cdd:PRK07580  56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAglagniTFEVGDLESLLGRFDTV-VCL 134

                         90       100       110
                 ....*....|....*....|....*....|.
gi 640471004 113 SSLVVQWCSDLRRALAELYRVTRpgGMILFS 143
Cdd:PRK07580 135 DVLIHYPQEDAARMLAHLASLTR--GSLIFT 163
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-182 4.52e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 51.27  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   30 LQREVGERLLKMGRNHP-GQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQQAADRYllgDIENIPLPAAAV 108
Cdd:pfam13489   5 RERLLADLLLRLLPKLPsPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQF---DEQEAAVPAGKF 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640471004  109 DICFSSLVVQWCSDLRRALAELYRVTRPGGMILFSTLATDSLY--QLADAWQQVDGERHVNdFLPSAQIAAACGDY 182
Cdd:pfam13489  82 DVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEAdrLLLEWPYLRPRNGHIS-LFSARSLKRLLEEA 156
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 44-138 9.94e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 51.82  E-value: 9.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  44 NHPGQQLLDAGCGTGYFSrrwreLG-------KQVTALDLAPGMLAFARQQQAAD--RYLLGDIENIPLPAAAVDICFSS 114
Cdd:PLN02490 111 SDRNLKVVDVGGGTGFTT-----LGivkhvdaKNVTILDQSPHQLAKAKQKEPLKecKIIEGDAEDLPFPTDYADRYVSA 185

                         90       100
                 ....*....|....*....|....
gi 640471004 115 LVVQWCSDLRRALAELYRVTRPGG 138
Cdd:PLN02490 186 GSIEYWPDPQRGIKEAYRVLKIGG 209
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
46-201 1.32e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 50.90  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   46 PGQQLLDAGCGTG----YFSRRWRELGKqVTALDLAPGMLAFARQQQAAD-----RYLLGDIENIPLPAAAVDICFSSLV 116
Cdd:pfam01209  42 RGNKFLDVAGGTGdwtfGLSDSAGSSGK-VVGLDINENMLKEGEKKAKEEgkyniEFLQGNAEELPFEDDSFDIVTISFG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  117 VQWCSDLRRALAELYRVTRPGGMIL---FSTLATDSLYQLADAWQqvdgeRHVNDFLPSAqIAAACGDYRhHLQEAWQtl 193
Cdd:pfam01209 121 LRNFPDYLKVLKEAFRVLKPGGRVVcleFSKPENPLLSQAYELYF-----KYVMPFMGKM-FAKSYKSYQ-YLQESIR-- 191


                  ....*...
gi 640471004  194 EYPDVMTL 201
Cdd:pfam01209 192 DFPDQKTL 199
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 47-143 3.29e-07

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 49.80  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   47 GQQLLDAGCGTGYFSRRWRELGKQVTALDLAPGMLAFARQQ-QAADRY-----LLGDIENIPLPAAAVdICFSSLVVQWC 120
Cdd:TIGR02021  56 GKRVLDAGCGTGLLSIELAKRGAIVKAVDISEQMVQMARNRaQGRDVAgnvefEVNDLLSLCGEFDIV-VCMDVLIHYPA 134

                          90       100
                  ....*....|....*....|...
gi 640471004  121 SDLRRALAELYRVTRpgGMILFS 143
Cdd:TIGR02021 135 SDMAKALGHLASLTK--ERVIFT 155
PRK05785 PRK05785
hypothetical protein; Provisional
 50-135 1.85e-05

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 44.68  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  50 LLDAGCGTGYFSRRWRELGKQ-VTALDLAPGMLafaRQQQAADRYLLGDIENIPLPAAAVDICFSSLVVQWCSDLRRALA 128
Cdd:PRK05785  55 VLDVAAGKGELSYHFKKVFKYyVVALDYAENML---KMNLVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIA 131


                 ....*..
gi 640471004 129 ELYRVTR 135
Cdd:PRK05785 132 EFTRVSR 138
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 38-144 2.57e-05

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 43.40  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  38 LLKMGRNHPGQQLLDAGCGTGYF--SRRWreLGKQVTALDLAPGMLAFARQ-----QQAADRYLLGDIENIPLPAAAVD- 109
Cdd:COG1041   18 LVNLAGAKEGDTVLDPFCGTGTIliEAGL--LGRRVIGSDIDPKMVEGAREnlehyGYEDADVIRGDARDLPLADESVDa 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 640471004 110 ICF-------SSLVVQWCSDL-RRALAELYRVTRPGGMILFST 144
Cdd:COG1041   96 IVTdppygrsSKISGEELLELyEKALEEAARVLKPGGRVVIVT 138
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
94-185 3.91e-05

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 42.93  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  94 LLGDIEN-IPLPAAAVDICFSSLVVQ--WCSDLRRALAELYRVTRPGGMILfstLATDSLYQLADAWQQVDGERHVNDFL 170
Cdd:COG4627   32 IVGDLTDpLPFPDNSVDAIYSSHVLEhlDYEEAPLALKECYRVLKPGGILR---IVVPDLEHVARLYLAEYDAALDVAEL 108

                         90
                 ....*....|....*
gi 640471004 171 PSAQIAAACGDYRHH 185
Cdd:COG4627  109 RLAGPIDPLGIILGE 123
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 48-159 5.78e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 43.39  E-value: 5.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  48 QQLLDAGCGTG----YFSRRWRelGKQVTALDLAPGMLAFARQQQAADRYLLGDIENIpLPAAAVDICFSSLVVQWCSDL 123
Cdd:PRK01683  33 RYVVDLGCGPGnsteLLVERWP--AARITGIDSSPAMLAEARSRLPDCQFVEADIASW-QPPQALDLIFANASLQWLPDH 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 640471004 124 RRALAELYRVTRPGGmilfsTLATdslyQLADAWQQ 159
Cdd:PRK01683 110 LELFPRLVSLLAPGG-----VLAV----QMPDNLDE 136
PLN02244 PLN02244
tocopherol O-methyltransferase
 51-144 2.28e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 41.65  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  51 LDAGCGTG----YFSRRWrelGKQVTALDLAPGML----AFARQQQAADR--YLLGDIENIPLPAAAVDICFSSLVVQWC 120
Cdd:PLN02244 123 VDVGCGIGgssrYLARKY---GANVKGITLSPVQAaranALAAAQGLSDKvsFQVADALNQPFEDGQFDLVWSMESGEHM 199

                         90       100
                 ....*....|....*....|....
gi 640471004 121 SDLRRALAELYRVTRPGGMILFST 144
Cdd:PLN02244 200 PDKRKFVQELARVAAPGGRIIIVT 223
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
46-104 6.51e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 39.50  E-value: 6.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640471004  46 PGQQLLDAGCGTGYFSRRWRELG-KQVTALDLAPGMLAFARqqQAADR------YLLGDIENIPLP 104
Cdd:COG2263   45 EGKTVLDLGCGTGMLAIGAALLGaKKVVGVDIDPEALEIAR--ENAERlgvrvdFIRADVTRIPLG 108
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 46-142 9.83e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.67  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTG----YFSRRWRelGKQVTALDLAPGMLAFARQQQAADRylLGDIENIpLPAAAVDICFSSLVVQWCS 121
Cdd:PRK14103  29 RARRVVDLGCGPGnltrYLARRWP--GAVIEALDSSPEMVAAARERGVDAR--TGDVRDW-KPKPDTDVVVSNAALQWVP 103

                         90       100
                 ....*....|....*....|....*
gi 640471004 122 D----LRRALAELyrvtRPGGMILF 142
Cdd:PRK14103 104 EhadlLVRWVDEL----APGSWIAV 124
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 31-141 1.89e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 37.31  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004   31 QREVGERLLKMGRNHPGQQLLDAGCGTGYFSRRWREL--GKQVTALDLAPGMLAFARQQqaADRYLLGDI----ENIPLP 104
Cdd:TIGR02469   4 KREVRALTLAKLRLRPGDVLWDIGAGTGSVTIEAARLvpNGRVYAIERNPEALDLIERN--LRRFGVSNIviveGDAPEA 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 640471004  105 AAAVDICFSSLVVQWCSD-LRRALAELYRVTRPGGMIL 141
Cdd:TIGR02469  82 PEALLPDPDAVFVGGSGGlLQEILEAVERRLRPGGRIV 119
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 46-143 3.03e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.58  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  46 PGQQLLDAGCGTG----YFSrrwRELGKQVTALDLAPGMLAFARQQ----QAADRYLLGDIENIPLPAAAVDICFSSLVV 117
Cdd:PLN02336 266 PGQKVLDVGCGIGggdfYMA---ENFDVHVVGIDLSVNMISFALERaigrKCSVEFEVADCTKKTYPDNSFDVIYSRDTI 342

                         90       100
                 ....*....|....*....|....*.
gi 640471004 118 QWCSDLRRALAELYRVTRPGGMILFS 143
Cdd:PLN02336 343 LHIQDKPALFRSFFKWLKPGGKVLIS 368
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
51-149 4.40e-03

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 37.92  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640471004  51 LDAGCGTGYFSrrWRELG---KQVTALDlaPGML---------AFARQQQAADRYLLGdIENIPlPAAAVDICFSSLVvq 118
Cdd:PRK15068 127 LDVGCGNGYHM--WRMLGagaKLVVGID--PSQLflcqfeavrKLLGNDQRAHLLPLG-IEQLP-ALKAFDTVFSMGV-- 198

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 640471004 119 wcsdL--RR----ALAELYRVTRPGGMILFSTLATDS 149
Cdd:PRK15068 199 ----LyhRRspldHLKQLKDQLVPGGELVLETLVIDG 231
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH